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folding</title> <meta name="description" content="Search results for: protein folding"> <meta name="keywords" content="protein folding"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar navbar-expand-lg navbar-light"> <a class="navbar-brand" href="https://waset.org"> <img src="https://cdn.waset.org/static/images/wasetc.png" alt="Open Science Research Excellence" title="Open Science Research Excellence" /> </a> <button class="d-block d-lg-none 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action="https://publications.waset.org/abstracts/search"> <div id="custom-search-input"> <div class="input-group"> <i class="fas fa-search"></i> <input type="text" class="search-query" name="q" placeholder="Author, Title, Abstract, Keywords" value="protein folding"> <input type="submit" class="btn_search" value="Search"> </div> </div> </form> </div> </div> <div class="row mt-3"> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Commenced</strong> in January 2007</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Frequency:</strong> Monthly</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Edition:</strong> International</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Paper Count:</strong> 2417</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: protein folding</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2417</span> In vitro Protein Folding and Stability Using Thermostable Exoshells </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Siddharth%20Deshpande">Siddharth Deshpande</a>, <a href="https://publications.waset.org/abstracts/search?q=Nihar%20Masurkar"> Nihar Masurkar</a>, <a href="https://publications.waset.org/abstracts/search?q=Vallerinteavide%20Mavelli%20Girish"> Vallerinteavide Mavelli Girish</a>, <a href="https://publications.waset.org/abstracts/search?q=Malan%20Desai"> Malan Desai</a>, <a href="https://publications.waset.org/abstracts/search?q=Chester%20Drum"> Chester Drum</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Folding and stabilization of recombinant proteins remain a consistent challenge for industrial and therapeutic applications. Proteins derived from thermophilic bacteria often have superior expression and stability qualities. To develop a generalizable approach to protein folding and stabilization, we tested the hypothesis that wrapping a thermostable exoshell around a protein substrate would aid folding and impart thermostable qualities to the internalized substrate. To test the effect of internalizing a protein within a thermostable exoshell (tES), we tested in vitro folding and stability using green fluorescent protein (GFPuv), horseradish peroxidase (HRP) and renilla luciferase (rLuc). The 8nm interior volume of a thermostable ferritin assembly was engineered to accommodate foreign proteins and either present a positive, neutral or negative interior charge environment. We further engineered the tES complex to reversibly assemble and disassemble with pH titration. Template proteins were expressed as inclusion bodies and an in vitro folding protocol was developed that forced proteins to fold inside a single tES. Functional yield was improved 100-fold, 100-fold and 150-fold with use of tES for GFPuv, HRP and rLuc respectively and was highly dependent on the internal charge environment of the tES. After folding, functional proteins could be released from the tES folding cavity using size exclusion chromatography at pH 5.8. Internalized proteins were tested for improved stability against thermal, organic, urea and guanidine denaturation. Our results demonstrated that thermostable exoshells can efficiently refold and stabilize inactive aggregates into functional proteins. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=thermostable%20shell" title="thermostable shell">thermostable shell</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vitro%20folding" title=" in vitro folding"> in vitro folding</a>, <a href="https://publications.waset.org/abstracts/search?q=stability" title=" stability"> stability</a>, <a href="https://publications.waset.org/abstracts/search?q=functional%20yield" title=" functional yield"> functional yield</a> </p> <a href="https://publications.waset.org/abstracts/72637/in-vitro-protein-folding-and-stability-using-thermostable-exoshells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/72637.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">249</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2416</span> Biophysical Characterization of Archaeal Cyclophilin Like Chaperone Protein</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Vineeta%20Kaushik">Vineeta Kaushik</a>, <a href="https://publications.waset.org/abstracts/search?q=Manisha%20Goel"> Manisha Goel</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Chaperones are proteins that help other proteins fold correctly, and are found in all domains of life i.e., prokaryotes, eukaryotes and archaea. Various comparative genomic studies have suggested that the archaeal protein folding machinery appears to be highly similar to that found in eukaryotes. In case of protein folding; slow rotation of peptide prolyl-imide bond is often the rate limiting step. Formation of the prolyl-imide bond during the folding of a protein requires the assistance of other proteins, termed as peptide prolyl cis-trans isomerases (PPIases). Cyclophilins constitute the class of peptide prolyl isomerases with a wide range of biological function like protein folding, signaling and chaperoning. Most of the cyclophilins exhibit PPIase enzymatic activity and play active role in substrate protein folding which classifies them as a category of molecular chaperones. Till date, there is not very much data available in the literature on archaeal cyclophilins. We aim to compare the structural and biochemical features of the cyclophilin protein from within the three domains to elucidate the features affecting their stability and enzyme activity. In the present study, we carry out in-silico analysis of the cyclophilin proteins to predict their conserved residues, sites under positive selection and compare these proteins to their bacterial and eukaryotic counterparts to predict functional divergence. We also aim to clone and express these proteins in heterologous system and study their biophysical characteristics in detail using techniques like CD and fluorescence spectroscopy. Overall we aim to understand the features contributing to the folding, stability and dynamics of the archaeal cyclophilin proteins. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biophysical%20characterization" title="biophysical characterization">biophysical characterization</a>, <a href="https://publications.waset.org/abstracts/search?q=x-ray%20crystallography" title=" x-ray crystallography"> x-ray crystallography</a>, <a href="https://publications.waset.org/abstracts/search?q=chaperone-like%20activity" title=" chaperone-like activity"> chaperone-like activity</a>, <a href="https://publications.waset.org/abstracts/search?q=cyclophilin" title=" cyclophilin"> cyclophilin</a>, <a href="https://publications.waset.org/abstracts/search?q=PPIase%20activity" title=" PPIase activity"> PPIase activity</a> </p> <a href="https://publications.waset.org/abstracts/67459/biophysical-characterization-of-archaeal-cyclophilin-like-chaperone-protein" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/67459.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">213</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2415</span> Insights of Interaction Studies between HSP-60, HSP-70 Proteins and HSF-1 in Bubalus bubalis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ravinder%20Singh">Ravinder Singh</a>, <a href="https://publications.waset.org/abstracts/search?q=C%20Rajesh"> C Rajesh</a>, <a href="https://publications.waset.org/abstracts/search?q=Saroj%20Badhan"> Saroj Badhan</a>, <a href="https://publications.waset.org/abstracts/search?q=Shailendra%20Mishra"> Shailendra Mishra</a>, <a href="https://publications.waset.org/abstracts/search?q=Ranjit%20Singh%20Kataria"> Ranjit Singh Kataria</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Heat shock protein 60 and 70 are crucial chaperones that guide appropriate folding of denatured proteins under heat stress conditions. HSP60 and HSP70 provide assistance in correct folding of a multitude of denatured proteins. The heat shock factors are the family of some transcription factors which controls the regulation of gene expression of proteins involved in folding of damaged or improper folded proteins during stress conditions. Under normal condition heat shock proteins bind with HSF-1 and act as its repressor as well as aids in maintaining the HSF-1’s nonactive and monomeric confirmation. The experimental protein structure for all these proteins in Bubalus bubalis is not known till date. Therefore computational approach was explored to identify three-dimensional structure analysis of all these proteins. In this study, an extensive in silico analysis has been performed including sequence comparison among species to comparative modeling of Bubalus bubalis HSP60, HSP70 and HSF-1 protein. The stereochemical properties of proteins were assessed by utilizing several scrutiny bioinformatics tools to ensure model accuracy. Further docking approach was used to study interactions between Heat shock proteins and HSF-1. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bubalus%20bubalis" title="Bubalus bubalis">Bubalus bubalis</a>, <a href="https://publications.waset.org/abstracts/search?q=comparative%20modelling" title=" comparative modelling"> comparative modelling</a>, <a href="https://publications.waset.org/abstracts/search?q=docking" title=" docking"> docking</a>, <a href="https://publications.waset.org/abstracts/search?q=heat%20shock%20protein" title=" heat shock protein"> heat shock protein</a> </p> <a href="https://publications.waset.org/abstracts/64431/insights-of-interaction-studies-between-hsp-60-hsp-70-proteins-and-hsf-1-in-bubalus-bubalis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/64431.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">322</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2414</span> Predicting Aggregation Propensity from Low-Temperature Conformational Fluctuations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hamza%20Javar%20Magnier">Hamza Javar Magnier</a>, <a href="https://publications.waset.org/abstracts/search?q=Robin%20Curtis"> Robin Curtis</a> </p> <p class="card-text"><strong>Abstract:</strong></p> There have been rapid advances in the upstream processing of protein therapeutics, which has shifted the bottleneck to downstream purification and formulation. Finding liquid formulations with shelf lives of up to two years is increasingly difficult for some of the newer therapeutics, which have been engineered for activity, but their formulations are often viscous, can phase separate, and have a high propensity for irreversible aggregation1. We explore means to develop improved predictive ability from a better understanding of how protein-protein interactions on formulation conditions (pH, ionic strength, buffer type, presence of excipients) and how these impact upon the initial steps in protein self-association and aggregation. In this work, we study the initial steps in the aggregation pathways using a minimal protein model based on square-well potentials and discontinuous molecular dynamics. The effect of model parameters, including range of interaction, stiffness, chain length, and chain sequence, implies that protein models fold according to various pathways. By reducing the range of interactions, the folding- and collapse- transition come together, and follow a single-step folding pathway from the denatured to the native state2. After parameterizing the model interaction-parameters, we developed an understanding of low-temperature conformational properties and fluctuations, and the correlation to the folding transition of proteins in isolation. The model fluctuations increase with temperature. We observe a low-temperature point, below which large fluctuations are frozen out. This implies that fluctuations at low-temperature can be correlated to the folding transition at the melting temperature. Because proteins “breath” at low temperatures, defining a native-state as a single structure with conserved contacts and a fixed three-dimensional structure is misleading. Rather, we introduce a new definition of a native-state ensemble based on our understanding of the core conservation, which takes into account the native fluctuations at low temperatures. This approach permits the study of a large range of length and time scales needed to link the molecular interactions to the macroscopically observed behaviour. In addition, these models studied are parameterized by fitting to experimentally observed protein-protein interactions characterized in terms of osmotic second virial coefficients. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20folding" title="protein folding">protein folding</a>, <a href="https://publications.waset.org/abstracts/search?q=native-ensemble" title=" native-ensemble"> native-ensemble</a>, <a href="https://publications.waset.org/abstracts/search?q=conformational%20fluctuation" title=" conformational fluctuation"> conformational fluctuation</a>, <a href="https://publications.waset.org/abstracts/search?q=aggregation" title=" aggregation"> aggregation</a> </p> <a href="https://publications.waset.org/abstracts/18844/predicting-aggregation-propensity-from-low-temperature-conformational-fluctuations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/18844.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">361</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2413</span> Folding Pathway and Thermodynamic Stability of Monomeric GroEL</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sarita%20Puri">Sarita Puri</a>, <a href="https://publications.waset.org/abstracts/search?q=Tapan%20K.%20Chaudhuri"> Tapan K. Chaudhuri</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Chaperonin GroEL is a tetradecameric Escherichia coli protein having identical subunits of 57 kDa. The elucidation of thermodynamic parameters related to stability for the native GroEL is not feasible as it undergoes irreversible unfolding because of its large size (800kDa) and multimeric nature. Nevertheless, it is important to determine the thermodynamic stability parameters for the highly stable GroEL protein as it helps in folding and holding of many substrate proteins during many cellular stresses. Properly folded monomers work as building-block for the formation of native tetradecameric GroEL. Spontaneous refolding behavior of monomeric GroEL makes it suitable for protein-denaturant interactions and thermodynamic stability based studies. The urea mediated unfolding is a three state process which means there is the formation of one intermediate state along with native and unfolded states. The heat mediated denaturation is a two-state process. The unfolding process is reversible as observed by the spontaneous refolding of denatured protein in both urea and head mediated refolding processes. Analysis of folding/unfolding data provides a measure of various thermodynamic stability parameters for the monomeric GroEL. The proposed mechanism of unfolding of monomeric GroEL is a three state process which involves formation of one stable intermediate having folded apical domain and unfolded equatorial, intermediate domains. Research in progress is to demonstrate the importance of specific residues in stability and oligomerization of GroEL protein. Several mutant versions of GroEL are under investigation to resolve the above mentioned issue. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=equilibrium%20unfolding" title="equilibrium unfolding">equilibrium unfolding</a>, <a href="https://publications.waset.org/abstracts/search?q=monomeric%20GroEl" title=" monomeric GroEl"> monomeric GroEl</a>, <a href="https://publications.waset.org/abstracts/search?q=spontaneous%20refolding" title=" spontaneous refolding"> spontaneous refolding</a>, <a href="https://publications.waset.org/abstracts/search?q=thermodynamic%20stability" title=" thermodynamic stability"> thermodynamic stability</a> </p> <a href="https://publications.waset.org/abstracts/67151/folding-pathway-and-thermodynamic-stability-of-monomeric-groel" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/67151.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">282</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2412</span> Folding of β-Structures via the Polarized Structure-Specific Backbone Charge (PSBC) Model</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Yew%20Mun%20Yip">Yew Mun Yip</a>, <a href="https://publications.waset.org/abstracts/search?q=Dawei%20Zhang"> Dawei Zhang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Proteins are the biological machinery that executes specific vital functions in every cell of the human body by folding into their 3D structures. When a protein misfolds from its native structure, the machinery will malfunction and lead to misfolding diseases. Although in vitro experiments are able to conclude that the mutations of the amino acid sequence lead to incorrectly folded protein structures, these experiments are unable to decipher the folding process. Therefore, molecular dynamic (MD) simulations are employed to simulate the folding process so that our improved understanding of the folding process will enable us to contemplate better treatments for misfolding diseases. MD simulations make use of force fields to simulate the folding process of peptides. Secondary structures are formed via the hydrogen bonds formed between the backbone atoms (C, O, N, H). It is important that the hydrogen bond energy computed during the MD simulation is accurate in order to direct the folding process to the native structure. Since the atoms involved in a hydrogen bond possess very dissimilar electronegativities, the more electronegative atom will attract greater electron density from the less electronegative atom towards itself. This is known as the polarization effect. Since the polarization effect changes the electron density of the two atoms in close proximity, the atomic charges of the two atoms should also vary based on the strength of the polarization effect. However, the fixed atomic charge scheme in force fields does not account for the polarization effect. In this study, we introduce the polarized structure-specific backbone charge (PSBC) model. The PSBC model accounts for the polarization effect in MD simulation by updating the atomic charges of the backbone hydrogen bond atoms according to equations derived between the amount of charge transferred to the atom and the length of the hydrogen bond, which are calculated from quantum-mechanical calculations. Compared to other polarizable models, the PSBC model does not require quantum-mechanical calculations of the peptide simulated at every time-step of the simulation and maintains the dynamic update of atomic charges, thereby reducing the computational cost and time while accounting for the polarization effect dynamically at the same time. The PSBC model is applied to two different β-peptides, namely the Beta3s/GS peptide, a de novo designed three-stranded β-sheet whose structure is folded in vitro and studied by NMR, and the trpzip peptides, a double-stranded β-sheet where a correlation is found between the type of amino acids that constitute the β-turn and the β-propensity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=hydrogen%20bond" title="hydrogen bond">hydrogen bond</a>, <a href="https://publications.waset.org/abstracts/search?q=polarization%20effect" title=" polarization effect"> polarization effect</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20folding" title=" protein folding"> protein folding</a>, <a href="https://publications.waset.org/abstracts/search?q=PSBC" title=" PSBC"> PSBC</a> </p> <a href="https://publications.waset.org/abstracts/45837/folding-of-v-structures-via-the-polarized-structure-specific-backbone-charge-psbc-model" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/45837.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">270</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2411</span> Protein Tertiary Structure Prediction by a Multiobjective Optimization and Neural Network Approach</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alexandre%20Barbosa%20de%20Almeida">Alexandre Barbosa de Almeida</a>, <a href="https://publications.waset.org/abstracts/search?q=Telma%20Woerle%20de%20Lima%20Soares"> Telma Woerle de Lima Soares</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Protein structure prediction is a challenging task in the bioinformatics field. The biological function of all proteins majorly relies on the shape of their three-dimensional conformational structure, but less than 1% of all known proteins in the world have their structure solved. This work proposes a deep learning model to address this problem, attempting to predict some aspects of the protein conformations. Throughout a process of multiobjective dominance, a recurrent neural network was trained to abstract the particular bias of each individual multiobjective algorithm, generating a heuristic that could be useful to predict some of the relevant aspects of the three-dimensional conformation process formation, known as protein folding. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ab%20initio%20heuristic%20modeling" title="Ab initio heuristic modeling">Ab initio heuristic modeling</a>, <a href="https://publications.waset.org/abstracts/search?q=multiobjective%20optimization" title=" multiobjective optimization"> multiobjective optimization</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20structure%20prediction" title=" protein structure prediction"> protein structure prediction</a>, <a href="https://publications.waset.org/abstracts/search?q=recurrent%20neural%20network" title=" recurrent neural network"> recurrent neural network</a> </p> <a href="https://publications.waset.org/abstracts/141565/protein-tertiary-structure-prediction-by-a-multiobjective-optimization-and-neural-network-approach" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/141565.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">205</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2410</span> Towards the Inhibition Mechanism of Lysozyme Fibrillation by Hydrogen Sulfide</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Indra%20Gonzalez%20Ojeda">Indra Gonzalez Ojeda</a>, <a href="https://publications.waset.org/abstracts/search?q=Tatiana%20Quinones"> Tatiana Quinones</a>, <a href="https://publications.waset.org/abstracts/search?q=Manuel%20Rosario"> Manuel Rosario</a>, <a href="https://publications.waset.org/abstracts/search?q=Igor%20Lednev"> Igor Lednev</a>, <a href="https://publications.waset.org/abstracts/search?q=Juan%20Lopez%20Garriga"> Juan Lopez Garriga</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Amyloid fibrils are stable aggregates of misfolded protein associated with many neurodegenerative disorders. It has been shown that hydrogen sulfide (H2S), inhibits the fibrillation of lysozyme through the formation of trisulfide (S-S-S) bonds. However, the overall mechanism remains elusive. Here, the concentration dependence of H2S effect was investigated using Atomic force microscopy (AFM), non-resonance Raman spectroscopy, Deep-UV Raman spectroscopy and circular dichroism (CD). It was found that small spherical aggregates with trisulfide bonds and a unique secondary structure were formed instead of amyloid fibrils when adding concentrations of 25 mM and 50 mM of H2S. This could indicate that H2S might serve as a protecting agent for the protein. However, further characterization of these aggregates and their trisulfide bonds is needed to fully unravel the function H2S has on protein fibrillation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amyloid%20fibrils" title="amyloid fibrils">amyloid fibrils</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrogen%20sulfide" title=" hydrogen sulfide"> hydrogen sulfide</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20folding" title=" protein folding"> protein folding</a>, <a href="https://publications.waset.org/abstracts/search?q=raman%20spectroscopy" title=" raman spectroscopy"> raman spectroscopy</a> </p> <a href="https://publications.waset.org/abstracts/86031/towards-the-inhibition-mechanism-of-lysozyme-fibrillation-by-hydrogen-sulfide" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/86031.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">216</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2409</span> Optical and Double Folding Model Analysis for Alpha Particles Elastically Scattered from 9Be and 11B Nuclei at Different Energies</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ahmed%20H.%20Amer">Ahmed H. Amer</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Amar"> A. Amar</a>, <a href="https://publications.waset.org/abstracts/search?q=Sh.%20Hamada"> Sh. Hamada</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20I.%20Bondouk"> I. I. Bondouk</a>, <a href="https://publications.waset.org/abstracts/search?q=F.%20A.%20El-Hussiny"> F. A. El-Hussiny</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Elastic scattering of α-particles from 9Be and 11B nuclei at different alpha energies have been analyzed. Optical model parameters (OMPs) of α-particles elastic scattering by these nuclei at different energies have been obtained. In the present calculations, the real part of the optical potential are derived by folding of nucleon-nucleon (NN) interaction into nuclear matter density distribution of the projectile and target nuclei using computer code FRESCO. A density-dependent version of the M3Y interaction (CDM3Y6), which is based on the G-matrix elements of the Paris NN potential, has been used. Volumetric integrals of the real and imaginary potential depth (JR, JW) have been calculated and found to be energy dependent. Good agreement between the experimental data and the theoretical predictions in the whole angular range. In double folding (DF) calculations, the obtained normalization coeﬃcient Nr is in the range 0.70–1.32. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=elastic%20scattering" title="elastic scattering">elastic scattering</a>, <a href="https://publications.waset.org/abstracts/search?q=optical%20model" title=" optical model"> optical model</a>, <a href="https://publications.waset.org/abstracts/search?q=double%20folding%20model" title=" double folding model"> double folding model</a>, <a href="https://publications.waset.org/abstracts/search?q=density%20distribution" title=" density distribution"> density distribution</a> </p> <a href="https://publications.waset.org/abstracts/45164/optical-and-double-folding-model-analysis-for-alpha-particles-elastically-scattered-from-9be-and-11b-nuclei-at-different-energies" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/45164.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">290</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2408</span> Optical and Double Folding Analysis for 6Li+16O Elastic Scattering</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Abd%20Elrahman%20Elgamala">Abd Elrahman Elgamala</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20Darwish"> N. Darwish</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20Bondouk"> I. Bondouk</a>, <a href="https://publications.waset.org/abstracts/search?q=Sh.%20Hamada"> Sh. Hamada</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Available experimental angular distributions for <sup>6</sup>Li elastically scattered from <sup>16</sup>O nucleus in the energy range 13.0–50.0 MeV are investigated and reanalyzed using optical model of the conventional phenomenological potential and also using double folding optical model of different interaction models: DDM3Y1, CDM3Y1, CDM3Y2, and CDM3Y3. All the involved models of interaction are of M3Y Paris except DDM3Y1 which is of M3Y Reid and the main difference between them lies in the different values for the parameters of the incorporated density distribution function <em>F</em>(ρ). We have extracted the renormalization factor <strong><em>N<sub>R</sub></em> </strong>for <sup>6</sup>Li+<sup>16</sup>O nuclear system in the energy range 13.0–50.0 MeV using the aforementioned interaction models. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=elastic%20scattering" title="elastic scattering">elastic scattering</a>, <a href="https://publications.waset.org/abstracts/search?q=optical%20model" title=" optical model"> optical model</a>, <a href="https://publications.waset.org/abstracts/search?q=folding%20potential" title=" folding potential"> folding potential</a>, <a href="https://publications.waset.org/abstracts/search?q=density%20distribution" title=" density distribution"> density distribution</a> </p> <a href="https://publications.waset.org/abstracts/132435/optical-and-double-folding-analysis-for-6li16o-elastic-scattering" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/132435.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">141</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2407</span> Kinetic Façade Design Using 3D Scanning to Convert Physical Models into Digital Models</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Do-Jin%20Jang">Do-Jin Jang</a>, <a href="https://publications.waset.org/abstracts/search?q=Sung-Ah%20Kim"> Sung-Ah Kim</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In designing a kinetic façade, it is hard for the designer to make digital models due to its complex geometry with motion. This paper aims to present a methodology of converting a point cloud of a physical model into a single digital model with a certain topology and motion. The method uses a Microsoft Kinect sensor, and color markers were defined and applied to three paper folding-inspired designs. Although the resulted digital model cannot represent the whole folding range of the physical model, the method supports the designer to conduct a performance-oriented design process with the rough physical model in the reduced folding range. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=design%20media" title="design media">design media</a>, <a href="https://publications.waset.org/abstracts/search?q=kinetic%20facades" title=" kinetic facades"> kinetic facades</a>, <a href="https://publications.waset.org/abstracts/search?q=tangible%20user%20interface" title=" tangible user interface"> tangible user interface</a>, <a href="https://publications.waset.org/abstracts/search?q=3D%20scanning" title=" 3D scanning"> 3D scanning</a> </p> <a href="https://publications.waset.org/abstracts/70846/kinetic-facade-design-using-3d-scanning-to-convert-physical-models-into-digital-models" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/70846.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">413</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2406</span> Further Investigation of α+12C and α+16O Elastic Scattering</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sh.%20Hamada">Sh. Hamada</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The current work aims to study the rainbow like-structure observed in the elastic scattering of alpha particles on both <sup>12</sup>C and <sup>16</sup>O nuclei. We reanalyzed the experimental elastic scattering angular distributions data for α+<sup>12</sup>C and α+<sup>16</sup>O nuclear systems at different energies using both optical model and double folding potential of different interaction models such as: CDM3Y1, DDM3Y1, CDM3Y6 and BDM3Y1. Potential created by BDM3Y1 interaction model has the shallowest depth which reflects the necessity to use higher renormalization factor (<strong><em>N<sub>r</sub></em></strong>). Both optical model and double folding potential of different interaction models fairly reproduce the experimental data. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=density%20distribution" title="density distribution">density distribution</a>, <a href="https://publications.waset.org/abstracts/search?q=double%20folding" title=" double folding"> double folding</a>, <a href="https://publications.waset.org/abstracts/search?q=elastic%20scattering" title=" elastic scattering"> elastic scattering</a>, <a href="https://publications.waset.org/abstracts/search?q=nuclear%20rainbow" title=" nuclear rainbow"> nuclear rainbow</a>, <a href="https://publications.waset.org/abstracts/search?q=optical%20model" title=" optical model"> optical model</a> </p> <a href="https://publications.waset.org/abstracts/61332/further-investigation-of-a12c-and-a16o-elastic-scattering" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/61332.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">237</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2405</span> Bioinformatics Approach to Identify Physicochemical and Structural Properties Associated with Successful Cell-free Protein Synthesis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alexander%20A.%20Tokmakov">Alexander A. Tokmakov</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cell-free protein synthesis is widely used to synthesize recombinant proteins. It allows genome-scale expression of various polypeptides under strictly controlled uniform conditions. However, only a minor fraction of all proteins can be successfully expressed in the systems of protein synthesis that are currently used. The factors determining expression success are poorly understood. At present, the vast volume of data is accumulated in cell-free expression databases. It makes possible comprehensive bioinformatics analysis and identification of multiple features associated with successful cell-free expression. Here, we describe an approach aimed at identification of multiple physicochemical and structural properties of amino acid sequences associated with protein solubility and aggregation and highlight major correlations obtained using this approach. The developed method includes: categorical assessment of the protein expression data, calculation and prediction of multiple properties of expressed amino acid sequences, correlation of the individual properties with the expression scores, and evaluation of statistical significance of the observed correlations. Using this approach, we revealed a number of statistically significant correlations between calculated and predicted features of protein sequences and their amenability to cell-free expression. It was found that some of the features, such as protein pI, hydrophobicity, presence of signal sequences, etc., are mostly related to protein solubility, whereas the others, such as protein length, number of disulfide bonds, content of secondary structure, etc., affect mainly the expression propensity. We also demonstrated that amenability of polypeptide sequences to cell-free expression correlates with the presence of multiple sites of post-translational modifications. The correlations revealed in this study provide a plethora of important insights into protein folding and rationalization of protein production. The developed bioinformatics approach can be of practical use for predicting expression success and optimizing cell-free protein synthesis. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=bioinformatics%20analysis" title="bioinformatics analysis">bioinformatics analysis</a>, <a href="https://publications.waset.org/abstracts/search?q=cell-free%20protein%20synthesis" title=" cell-free protein synthesis"> cell-free protein synthesis</a>, <a href="https://publications.waset.org/abstracts/search?q=expression%20success" title=" expression success"> expression success</a>, <a href="https://publications.waset.org/abstracts/search?q=optimization" title=" optimization"> optimization</a>, <a href="https://publications.waset.org/abstracts/search?q=recombinant%20proteins" title=" recombinant proteins"> recombinant proteins</a> </p> <a href="https://publications.waset.org/abstracts/22904/bioinformatics-approach-to-identify-physicochemical-and-structural-properties-associated-with-successful-cell-free-protein-synthesis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/22904.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">419</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2404</span> The Development of an Automated Computational Workflow to Prioritize Potential Resistance Variants in HIV Integrase Subtype C</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Keaghan%20Brown">Keaghan Brown</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The prioritization of drug resistance mutations impacting protein folding or protein-drug and protein-DNA interactions within macromolecular systems is critical to the success of treatment regimens. With a continual increase in computational tools to assess these impacts, the need for scalability and reproducibility became an essential component of computational analysis and experimental research. Here it introduce a bioinformatics pipeline that combines several structural analysis tools in a simplified workflow, by optimizing the present computational hardware and software to automatically ease the flow of data transformations. Utilizing preestablished software tools, it was possible to develop a pipeline with a set of pre-defined functions that will automate mutation introduction into the HIV-1 Integrase protein structure, calculate the gain and loss of polar interactions and calculate the change in energy of protein fold. Additionally, an automated molecular dynamics analysis was implemented which reduces the constant need for user input and output management. The resulting pipeline, Automated Mutation Introduction and Analysis (AMIA) is an open source set of scripts designed to introduce and analyse the effects of mutations on the static protein structure as well as the results of the multi-conformational states from molecular dynamic simulations. The workflow allows the user to visualize all outputs in a user friendly manner thereby successfully enabling the prioritization of variant systems for experimental validation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=automated%20workflow" title="automated workflow">automated workflow</a>, <a href="https://publications.waset.org/abstracts/search?q=variant%20prioritization" title=" variant prioritization"> variant prioritization</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20resistance" title=" drug resistance"> drug resistance</a>, <a href="https://publications.waset.org/abstracts/search?q=HIV%20Integrase" title=" HIV Integrase"> HIV Integrase</a> </p> <a href="https://publications.waset.org/abstracts/178777/the-development-of-an-automated-computational-workflow-to-prioritize-potential-resistance-variants-in-hiv-integrase-subtype-c" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/178777.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">77</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2403</span> Computational Prediction of the Effect of S477N Mutation on the RBD Binding Affinity and Structural Characteristic, A Molecular Dynamics Study</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohammad%20Hossein%20Modarressi">Mohammad Hossein Modarressi</a>, <a href="https://publications.waset.org/abstracts/search?q=Mozhgan%20Mondeali"> Mozhgan Mondeali</a>, <a href="https://publications.waset.org/abstracts/search?q=Khabat%20Barkhordari"> Khabat Barkhordari</a>, <a href="https://publications.waset.org/abstracts/search?q=Ali%20Etemadi"> Ali Etemadi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The COVID-19 pandemic, caused by SARS-CoV-2, has led to significant concerns worldwide due to its catastrophic effects on public health. The SARS-CoV-2 infection is initiated with the binding of the receptor-binding domain (RBD) in its spike protein to the ACE2 receptor in the host cell membrane. Due to the error-prone entity of the viral RNA-dependent polymerase complex, the virus genome, including the coding region for the RBD, acquires new mutations, leading to the appearance of multiple variants. These variants can potentially impact transmission, virulence, antigenicity and evasive immune properties. S477N mutation located in the RBD has been observed in the SARS-CoV-2 omicron (B.1.1. 529) variant. In this study, we investigated the consequences of S477N mutation at the molecular level using computational approaches such as molecular dynamics simulation, protein-protein interaction analysis, immunoinformatics and free energy computation. We showed that displacement of Ser with Asn increases the stability of the spike protein and its affinity to ACE2 and thus increases the transmission potential of the virus. This mutation changes the folding and secondary structure of the spike protein. Also, it reduces antibody neutralization, raising concern about re-infection, vaccine breakthrough and therapeutic values. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=S477N" title="S477N">S477N</a>, <a href="https://publications.waset.org/abstracts/search?q=COVID-19" title=" COVID-19"> COVID-19</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamic" title=" molecular dynamic"> molecular dynamic</a>, <a href="https://publications.waset.org/abstracts/search?q=SARS-COV2%20mutations" title=" SARS-COV2 mutations"> SARS-COV2 mutations</a> </p> <a href="https://publications.waset.org/abstracts/145533/computational-prediction-of-the-effect-of-s477n-mutation-on-the-rbd-binding-affinity-and-structural-characteristic-a-molecular-dynamics-study" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/145533.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">176</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2402</span> Computational Approach for Grp78–Nf-ΚB Binding Interactions in the Context of Neuroprotective Pathway in Brain Injuries</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Janneth%20Gonzalez">Janneth Gonzalez</a>, <a href="https://publications.waset.org/abstracts/search?q=Marco%20Avila"> Marco Avila</a>, <a href="https://publications.waset.org/abstracts/search?q=George%20Barreto"> George Barreto</a> </p> <p class="card-text"><strong>Abstract:</strong></p> GRP78 participates in multiple functions in the cell during normal and pathological conditions, controlling calcium homeostasis, protein folding and unfolded protein response. GRP78 is located in the endoplasmic reticulum, but it can change its location under stress, hypoxic and apoptotic conditions. NF-κB represents the keystone of the inflammatory process and regulates the transcription of several genes related with apoptosis, differentiation, and cell growth. The possible relationship between GRP78-NF-κB could support and explain several mechanisms that may regulate a variety of cell functions, especially following brain injuries. Although several reports show interactions between NF-κB and heat shock proteins family members, there is a lack of information on how GRP78 may be interacting with NF-κB, and possibly regulating its downstream activation. Therefore, we assessed the computational predictions of the GRP78 (Chain A) and NF-κB complex (IkB alpha and p65) protein-protein interactions. The interaction interface of the docking model showed that the amino acids ASN 47, GLU 215, GLY 403 of GRP78 and THR 54, ASN 182 and HIS 184 of NF-κB are key residues involved in the docking. The electrostatic field between GRP78-NF-κB interfaces and molecular dynamic simulations support the possible interaction between the proteins. In conclusion, this work shed some light in the possible GRP78-NF-κB complex indicating key residues in this crosstalk, which may be used as an input for better drug design strategy targeting NF-κB downstream signaling as a new therapeutic approach following brain injuries. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=computational%20biology" title="computational biology">computational biology</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20interactions" title=" protein interactions"> protein interactions</a>, <a href="https://publications.waset.org/abstracts/search?q=Grp78" title=" Grp78"> Grp78</a>, <a href="https://publications.waset.org/abstracts/search?q=bioinformatics" title=" bioinformatics"> bioinformatics</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamics" title=" molecular dynamics "> molecular dynamics </a> </p> <a href="https://publications.waset.org/abstracts/29173/computational-approach-for-grp78-nf-kb-binding-interactions-in-the-context-of-neuroprotective-pathway-in-brain-injuries" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/29173.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">342</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2401</span> Enhanced Functional Production of a Crucial Biomolecule Human Serum Albumin in Escherichia coli</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ashima%20Sharma">Ashima Sharma</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Human Serum Albumin (HSA)- one of the most demanded therapeutic proteins with immense biotechnological applications- is a large multidomain protein containing 17 disulfide bonds. The current source of HSA is human blood plasma which is a limited and unsafe source. Thus, there exists an indispensable need to promote non-animal derived recombinant HSA (rHSA) production. Escherichia coli is one of the most convenient hosts which had contributed to the production of more than 30% of the FDA approved recombinant pharmaceuticals. It grows rapidly and reaches high cell density using inexpensive and simple substrates. E. coli derived recombinant products have more economic potential as fermentation processes are cheaper compared to the other expression hosts. The major bottleneck in exploiting E. coli as a host for a disulfide-rich multidomain protein is the formation of aggregates of overexpressed protein. The majority of the expressed HSA forms inclusion bodies (more than 90% of the total expressed rHSA) in the E. coli cytosol. Recovery of functional rHSA from inclusion bodies is not preferred because it is difficult to obtain a large multidomain disulfide bond rich protein like rHSA in its functional native form. Purification is tedious, time-consuming, laborious and expensive. Because of such limitations, the E. coli host system was neglected for rHSA production for the past few decades despite its numerous advantages. In the present work, we have exploited the capabilities of E. coli as a host for the enhanced functional production of rHSA (~60% of the total expressed rHSA in the soluble fraction). Parameters like intracellular environment, temperature, induction type, duration of induction, cell lysis conditions etc. which play an important role in enhancing the level of production of the desired protein in its native form in vivo have been optimized. We have studied the effect of assistance of different types of exogenously employed chaperone systems on the functional expression of rHSA in the E. coli host system. Different aspects of cell growth parameters during the production of rHSA in presence and absence of molecular chaperones in E. coli have also been studied. Upon overcoming the difficulties to produce functional rHSA in E. coli, it has been possible to produce significant levels of functional protein through engineering the biological system of protein folding in the cell, the E. coli-derived rHSA has been purified to homogeneity. Its detailed physicochemical characterization has been performed by monitoring its conformational properties, secondary and tertiary structure elements, surface properties, ligand binding properties, stability issues etc. These parameters of the recombinant protein have been compared with the naturally occurring protein from the human source. The outcome of the comparison reveals that the recombinant protein resembles exactly the same as the natural one. Hence, we propose that the E. coli-derived rHSA is an ideal biosimilar for human blood plasma-derived serum albumin. Therefore, in the present study, we have introduced and promoted the E. coli- derived rHSA as an alternative to the preparation from a human source, pHSA. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=recombinant%20human%20serum%20albumin" title="recombinant human serum albumin">recombinant human serum albumin</a>, <a href="https://publications.waset.org/abstracts/search?q=Escherichia%20coli" title=" Escherichia coli"> Escherichia coli</a>, <a href="https://publications.waset.org/abstracts/search?q=biosimilar" title=" biosimilar"> biosimilar</a>, <a href="https://publications.waset.org/abstracts/search?q=chaperone%20assisted%20protein%20folding" title=" chaperone assisted protein folding"> chaperone assisted protein folding</a> </p> <a href="https://publications.waset.org/abstracts/89334/enhanced-functional-production-of-a-crucial-biomolecule-human-serum-albumin-in-escherichia-coli" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/89334.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">209</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2400</span> Lentil Protein Fortification in Cranberry Squash</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sandhya%20Devi%20A">Sandhya Devi A</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The protein content of the cranberry squash (protein: 0g) may be increased by extracting protein from the lentils (9 g), which is particularly linked to a lower risk of developing heart disease. Using the technique of alkaline extraction from the lentils flour, protein may be extracted. Alkaline extraction of protein from lentil flour was optimized utilizing response surface approach in order to maximize both protein content and yield. Cranberry squash may be taken if a protein fortification syrup is prepared and processed into the squash. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alkaline%20extraction" title="alkaline extraction">alkaline extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=cranberry%20squash" title=" cranberry squash"> cranberry squash</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20fortification" title=" protein fortification"> protein fortification</a>, <a href="https://publications.waset.org/abstracts/search?q=response%20surface%20methodology" title=" response surface methodology"> response surface methodology</a> </p> <a href="https://publications.waset.org/abstracts/153178/lentil-protein-fortification-in-cranberry-squash" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/153178.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">111</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2399</span> Characterization of the GntR Family Transcriptional Regulator Rv0792c: A Potential Drug Target for Mycobacterium tuberculosis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Thanusha%20D.%20Abeywickrama">Thanusha D. Abeywickrama</a>, <a href="https://publications.waset.org/abstracts/search?q=Inoka%20C.%20Perera"> Inoka C. Perera</a>, <a href="https://publications.waset.org/abstracts/search?q=Genji%20Kurisu"> Genji Kurisu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Tuberculosis, considered being as the ninth leading cause of death worldwide, cause from a single infectious agent M. tuberculosis and the drug resistance nature of this bacterium is a continuing threat to the world. Therefore TB preventing treatment is expanding, where this study designed to analyze the regulatory mechanism of GntR transcriptional regulator gene Rv0792c, which lie between several genes codes for some hypothetical proteins, a monooxygenase and an oxidoreductase. The gene encoding Rv0792c was cloned into pET28a and expressed protein was purified to near homogeneity by Nickel affinity chromatography. It was previously reported that the protein binds within the intergenic region (BS region) between Rv0792c gene and monooxygenase (Rv0793). This resulted in binding of three protein molecules with the BS region suggesting tight control of monooxygenase as well as its own gene. Since monooxygenase plays a key role in metabolism, this gene may have a global regulatory role. The natural ligand for this regulator is still under investigation. In relation to the Rv0792 protein structure, a Circular Dichroism (CD) spectrum was carried out to determine its secondary structure elements. Percentage-wise, 17.4% Helix, 21.8% Antiparallel, 5.1% Parallel, 12.3% turn and 43.5% other were revealed from CD spectrum data under room temperature. Differential Scanning Calorimetry (DSC) was conducted to assess the thermal stability of Rv0792, which the melting temperature of protein is 57.2 ± 0.6 °C. The graph of heat capacity (Cp) versus temperature for the best fit was obtained for non-two-state model, which concludes the folding of Rv0792 protein occurs through stable intermediates. Peak area (∆HCal ) and Peak shape (∆HVant ) was calculated from the graph and ∆HCal / ∆HVant was close to 0.5, suggesting dimeric nature of the protein. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=CD%20spectrum" title="CD spectrum">CD spectrum</a>, <a href="https://publications.waset.org/abstracts/search?q=DSC%20analysis" title=" DSC analysis"> DSC analysis</a>, <a href="https://publications.waset.org/abstracts/search?q=GntR%20transcriptional%20regulator" title=" GntR transcriptional regulator"> GntR transcriptional regulator</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20structure" title=" protein structure"> protein structure</a> </p> <a href="https://publications.waset.org/abstracts/88842/characterization-of-the-gntr-family-transcriptional-regulator-rv0792c-a-potential-drug-target-for-mycobacterium-tuberculosis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/88842.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">222</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2398</span> Preferred Left-Handed Conformation of Glycyls at Pathogenic Sites</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Purva%20Mishra">Purva Mishra</a>, <a href="https://publications.waset.org/abstracts/search?q=Rajesh%20Potlia"> Rajesh Potlia</a>, <a href="https://publications.waset.org/abstracts/search?q=Kuljeet%20Singh%20Sandhu"> Kuljeet Singh Sandhu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The role of glycyl residues in the protein structure has lingered within the research community for the last several decades. Glycyl residue is the only amino acid that is achiral due to the lack of a side chain and can, therefore, exhibit Ramachandran conformations that are disallowed for L-amino acids. The structural and functional significance of glycyl residues with L-disallowed conformation, however, remains obscure. Through statistical analysis of various datasets, we found that the glycyls with L-disallowed conformations are over-represented at disease-associated sites and tend to be evolutionarily conserved. The mutations of L-disallowed glycyls tend to destabilize the native conformation, reduce protein solubility, and promote inter-molecular aggregations. We uncovered a structural motif referred to as “β-crescent” formed around the L-disallowed glycyl, which prevents β-sheet aggregation by disrupting the alternating pattern of β-pleats. The L-disallowed conformation of glycyls also holds predictive power to infer the pathogenic missense variants. Altogether, our observations highlight that the L-disallowed conformation of glycyls is selected to facilitate native folding and prevent inter-molecular aggregations. The findings may also have implications for designing more stable proteins and prioritizing the genetic lesions implicated in diseases. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ramachandran%20plot" title="Ramachandran plot">Ramachandran plot</a>, <a href="https://publications.waset.org/abstracts/search?q=%CE%B2-sheet" title=" β-sheet"> β-sheet</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20stability" title=" protein stability"> protein stability</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20aggregation" title=" protein aggregation"> protein aggregation</a> </p> <a href="https://publications.waset.org/abstracts/179122/preferred-left-handed-conformation-of-glycyls-at-pathogenic-sites" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/179122.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">72</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2397</span> Hydration of Protein-RNA Recognition Sites</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Amita%20Barik">Amita Barik</a>, <a href="https://publications.waset.org/abstracts/search?q=Ranjit%20Prasad%20Bahadur"> Ranjit Prasad Bahadur</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We investigate the role of water molecules in 89 protein-RNA complexes taken from the Protein Data Bank. Those with tRNA and single-stranded RNA are less hydrated than with duplex or ribosomal proteins. Protein-RNA interfaces are hydrated less than protein-DNA interfaces, but more than protein-protein interfaces. Majority of the waters at protein-RNA interfaces makes multiple H-bonds; however, a fraction does not make any. Those making Hbonds have preferences for the polar groups of RNA than its partner protein. The spatial distribution of waters makes interfaces with ribosomal proteins and single-stranded RNA relatively ‘dry’ than interfaces with tRNA and duplex RNA. In contrast to protein-DNA interfaces, mainly due to the presence of the 2’OH, the ribose in protein-RNA interfaces is hydrated more than the phosphate or the bases. The minor groove in protein-RNA interfaces is hydrated more than the major groove, while in protein-DNA interfaces it is reverse. The strands make the highest number of water-mediated H-bonds per unit interface area followed by the helices and the non-regular structures. The preserved waters at protein-RNA interfaces make higher number of H-bonds than the other waters. Preserved waters contribute toward the affinity in protein-RNA recognition and should be carefully treated while engineering protein-RNA interfaces. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=h-bonds" title="h-bonds">h-bonds</a>, <a href="https://publications.waset.org/abstracts/search?q=minor-major%20grooves" title=" minor-major grooves"> minor-major grooves</a>, <a href="https://publications.waset.org/abstracts/search?q=preserved%20water" title=" preserved water"> preserved water</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-RNA%20interfaces" title=" protein-RNA interfaces"> protein-RNA interfaces</a> </p> <a href="https://publications.waset.org/abstracts/42932/hydration-of-protein-rna-recognition-sites" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/42932.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">302</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2396</span> Protein Crystallization Induced by Surface Plasmon Resonance</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tetsuo%20Okutsu">Tetsuo Okutsu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We have developed a crystallization plate with the function of promoting protein crystallization. A gold thin film is deposited on the crystallization plate. A protein solution is dropped thereon, and crystallization is promoted when the protein is irradiated with light of a wavelength that protein does not absorb. Protein is densely adsorbed on the gold thin film surface. The light excites the surface plasmon resonance of the gold thin film, the protein is excited by the generated enhanced electric field induced by surface plasmon resonance, and the amino acid residues are radicalized to produce protein dimers. The dimers function as templates for protein crystals, crystallization is promoted. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=lysozyme" title="lysozyme">lysozyme</a>, <a href="https://publications.waset.org/abstracts/search?q=plasmon" title=" plasmon"> plasmon</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=crystallization" title=" crystallization"> crystallization</a>, <a href="https://publications.waset.org/abstracts/search?q=RNaseA" title=" RNaseA"> RNaseA</a> </p> <a href="https://publications.waset.org/abstracts/85433/protein-crystallization-induced-by-surface-plasmon-resonance" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/85433.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">218</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2395</span> Protein Remote Homology Detection and Fold Recognition by Combining Profiles with Kernel Methods</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bin%20Liu">Bin Liu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Protein remote homology detection and fold recognition are two most important tasks in protein sequence analysis, which is critical for protein structure and function studies. In this study, we combined the profile-based features with various string kernels, and constructed several computational predictors for protein remote homology detection and fold recognition. Experimental results on two widely used benchmark datasets showed that these methods outperformed the competing methods, indicating that these predictors are useful computational tools for protein sequence analysis. By analyzing the discriminative features of the training models, some interesting patterns were discovered, reflecting the characteristics of protein superfamilies and folds, which are important for the researchers who are interested in finding the patterns of protein folds. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20remote%20homology%20detection" title="protein remote homology detection">protein remote homology detection</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20fold%20recognition" title=" protein fold recognition"> protein fold recognition</a>, <a href="https://publications.waset.org/abstracts/search?q=profile-based%20features" title=" profile-based features"> profile-based features</a>, <a href="https://publications.waset.org/abstracts/search?q=Support%20Vector%20Machines%20%28SVMs%29" title=" Support Vector Machines (SVMs)"> Support Vector Machines (SVMs)</a> </p> <a href="https://publications.waset.org/abstracts/104054/protein-remote-homology-detection-and-fold-recognition-by-combining-profiles-with-kernel-methods" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/104054.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">161</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2394</span> Structural and Functional Comparison of Untagged and Tagged EmrE Protein</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=S.%20Junaid%20S.%20Qazi">S. Junaid S. Qazi</a>, <a href="https://publications.waset.org/abstracts/search?q=Denice%20C.%20Bay"> Denice C. Bay</a>, <a href="https://publications.waset.org/abstracts/search?q=Raymond%20Chew"> Raymond Chew</a>, <a href="https://publications.waset.org/abstracts/search?q=Raymond%20J.%20Turner"> Raymond J. Turner</a> </p> <p class="card-text"><strong>Abstract:</strong></p> EmrE, a member of the small multidrug resistance protein family in bacteria is considered to be the archetypical member of its family. It confers host resistance to a wide variety of quaternary cation compounds (QCCs) driven by proton motive force. Generally, purification yield is a challenge in all membrane proteins because of the difficulties in their expression, isolation and solubilization. EmrE is extremely hydrophobic which make the purification yield challenging. We have purified EmrE protein using two different approaches: organic solvent membrane extraction and hexahistidine (his6) tagged Ni-affinity chromatographic methods. We have characterized changes present between ligand affinity of untagged and his6-tagged EmrE proteins in similar membrane mimetic environments using biophysical experimental techniques. Purified proteins were solubilized in a buffer containing n-dodecyl-β-D-maltopyranoside (DDM) and the conformations in the proteins were explored in the presence of four QCCs, methyl viologen (MV), ethidium bromide (EB), cetylpyridinium chloride (CTP) and tetraphenyl phosphonium (TPP). SDS-Tricine PAGE and dynamic light scattering (DLS) analysis revealed that the addition of QCCs did not induce higher multimeric forms of either proteins at all QCC:EmrE molar ratios examined under the solubilization conditions applied. QCC binding curves obtained from the Trp fluorescence quenching spectra, gave the values of dissociation constant (Kd) and maximum specific one-site binding (Bmax). Lower Bmax values to QCCs for his6-tagged EmrE shows that the binding sites remained unoccupied. This lower saturation suggests that the his6-tagged versions provide a conformation that prevents saturated binding. Our data demonstrate that tagging an integral membrane protein can significantly influence the protein. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=small%20multidrug%20resistance%20%28SMR%29%20protein" title="small multidrug resistance (SMR) protein">small multidrug resistance (SMR) protein</a>, <a href="https://publications.waset.org/abstracts/search?q=EmrE" title=" EmrE"> EmrE</a>, <a href="https://publications.waset.org/abstracts/search?q=integral%20membrane%20protein%20folding" title=" integral membrane protein folding"> integral membrane protein folding</a>, <a href="https://publications.waset.org/abstracts/search?q=quaternary%20ammonium%20compounds%20%28QAC%29" title=" quaternary ammonium compounds (QAC)"> quaternary ammonium compounds (QAC)</a>, <a href="https://publications.waset.org/abstracts/search?q=quaternary%20cation%20compounds%20%28QCC%29" title=" quaternary cation compounds (QCC)"> quaternary cation compounds (QCC)</a>, <a href="https://publications.waset.org/abstracts/search?q=nickel%20affinity%20chromatography" title=" nickel affinity chromatography"> nickel affinity chromatography</a>, <a href="https://publications.waset.org/abstracts/search?q=hexahistidine%20%28His6%29%20tag" title=" hexahistidine (His6) tag"> hexahistidine (His6) tag</a> </p> <a href="https://publications.waset.org/abstracts/36260/structural-and-functional-comparison-of-untagged-and-tagged-emre-protein" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/36260.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">379</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2393</span> CAP-Glycine Protein Governs Growth, Differentiation, and the Pathogenicity of Global Meningoencephalitis Fungi</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Kyung-Tae%20Lee">Kyung-Tae Lee</a>, <a href="https://publications.waset.org/abstracts/search?q=Li%20Li%20Wang"> Li Li Wang</a>, <a href="https://publications.waset.org/abstracts/search?q=Kwang-Woo%20Jung"> Kwang-Woo Jung</a>, <a href="https://publications.waset.org/abstracts/search?q=Yong-Sun%20Bahn"> Yong-Sun Bahn</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Microtubules are involved in mechanical support, cytoplasmic organization as well as in a number of cellular processes by interacting with diverse microtubule-associated proteins (MAPs), such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A common feature of these proteins is the presence of a cytoskeleton-associated protein-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate functions of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which causes fatal meningoencephalitis globally. In this study, we identified five CAP-Gly proteins encoding genes in C. neoformans. Among these, Cgp1, encoded by CNAG_06352, has a unique domain structure that has not been reported before in other eukaryotes. Supporting the role of Cpg1 in microtubule-related functions, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer, and Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular functions of microtubules, Cgp1 also governs maintenance of membrane stability and genotoxic stress responses. Furthermore, we demonstrate that Cgp1 uniquely regulates sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Our domain analysis reveals that the CAP-Gly domain plays major roles in all the functions of Cgp1. Finally, the cgp1Δ mutant is attenuated in virulence. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation and pathogenicity of C. neoformans. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=human%20fungal%20pathogen" title="human fungal pathogen">human fungal pathogen</a>, <a href="https://publications.waset.org/abstracts/search?q=CAP-Glycine%20protein" title=" CAP-Glycine protein"> CAP-Glycine protein</a>, <a href="https://publications.waset.org/abstracts/search?q=microtubule" title=" microtubule"> microtubule</a>, <a href="https://publications.waset.org/abstracts/search?q=meningoencephalitis" title=" meningoencephalitis"> meningoencephalitis</a> </p> <a href="https://publications.waset.org/abstracts/63213/cap-glycine-protein-governs-growth-differentiation-and-the-pathogenicity-of-global-meningoencephalitis-fungi" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/63213.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">315</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2392</span> Membrane Spanning DNA Origami Nanopores for Protein Translocation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Genevieve%20Pugh">Genevieve Pugh</a>, <a href="https://publications.waset.org/abstracts/search?q=Johnathan%20Burns"> Johnathan Burns</a>, <a href="https://publications.waset.org/abstracts/search?q=Stefan%20Howorka"> Stefan Howorka</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Single-molecule sensing via protein nanopores has achieved a step-change in portable and label-free DNA sequencing. However, protein pores of both natural or engineered origin are not able to produce the tunable diameters needed for effective protein sensing. Here, we describe a generic strategy to build synthetic DNA nanopores that are wide enough to accommodate folded protein. The pores are composed of interlinked DNA duplexes and carry lipid anchors to achieve the required membrane insertion. Our demonstrator pore has a contiguous cross-sectional channel area of 50 nm2 which is 6-times larger than the largest protein pore. Consequently, transport of folded protein across bilayers is possible. The modular design is amenable for different pore dimensions and can be adapted for protein sensing or to create molecular gates in synthetic biology. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biosensing" title="biosensing">biosensing</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20nanotechnology" title=" DNA nanotechnology"> DNA nanotechnology</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20origami" title=" DNA origami"> DNA origami</a>, <a href="https://publications.waset.org/abstracts/search?q=nanopore%20sensing" title=" nanopore sensing"> nanopore sensing</a> </p> <a href="https://publications.waset.org/abstracts/78556/membrane-spanning-dna-origami-nanopores-for-protein-translocation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/78556.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">323</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2391</span> Clusterization Probability in 14N Nuclei</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=N.%20Burtebayev">N. Burtebayev</a>, <a href="https://publications.waset.org/abstracts/search?q=Sh.%20Hamada"> Sh. Hamada</a>, <a href="https://publications.waset.org/abstracts/search?q=Zh.%20Kerimkulov"> Zh. Kerimkulov</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20K.%20Alimov"> D. K. Alimov</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20V.%20Yushkov"> A. V. Yushkov</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20Amangeldi"> N. Amangeldi</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20N.%20Bakhtibaev"> A. N. Bakhtibaev</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The main aim of the current work is to examine if 14N is candidate to be clusterized nuclei or not. In order to check this attendance, we have measured the angular distributions for 14N ion beam elastically scattered on 12C target nuclei at different low energies; 17.5, 21, and 24.5MeV which are close to the Coulomb barrier energy for 14N+12C nuclear system. Study of various transfer reactions could provide us with useful information about the attendance of nuclei to be in a composite form (core + valence). The experimental data were analyzed using two approaches; Phenomenological (Optical Potential) and semi-microscopic (Double Folding Potential). The agreement between the experimental data and the theoretical predictions is fairly good in the whole angular range. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=deuteron%20transfer" title="deuteron transfer">deuteron transfer</a>, <a href="https://publications.waset.org/abstracts/search?q=elastic%20scattering" title=" elastic scattering"> elastic scattering</a>, <a href="https://publications.waset.org/abstracts/search?q=optical%20model" title=" optical model"> optical model</a>, <a href="https://publications.waset.org/abstracts/search?q=double%20folding" title=" double folding"> double folding</a>, <a href="https://publications.waset.org/abstracts/search?q=density%20distribution" title=" density distribution"> density distribution</a> </p> <a href="https://publications.waset.org/abstracts/2435/clusterization-probability-in-14n-nuclei" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2435.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">327</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2390</span> Promoting Creative and Critical Thinking in Mathematics</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ana%20Maria%20Reis%20D%27Azevedo%20Breda">Ana Maria Reis D'Azevedo Breda</a>, <a href="https://publications.waset.org/abstracts/search?q=Catarina%20Maria%20Neto%20da%20Cruz"> Catarina Maria Neto da Cruz</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The Japanese art of origami provides a rich context for designing exploratory mathematical activities for children and young people. By folding a simple sheet of paper, fascinating and surprising planar and spatial configurations emerge. Equally surprising is the unfolding process, which also produces striking patterns. The procedure of folding, unfolding, and folding again allows the exploration of interesting geometric patterns. When adequately and systematically done, we may deduce some of the mathematical rules ruling origami. As the child/youth folds the sheet of paper repeatedly, he can physically observe how the forms he obtains are transformed and how they relate to the pattern of the corresponding unfolding, creating space for the understanding/discovery of mathematical principles regulating the folding-unfolding process. As part of a 2023 Summer Academy organized by a Portuguese university, a session entitled “Folding, Thinking and Generalizing” took place. Twenty-three students attended the session, all enrolled in the 2nd cycle of Portuguese Basic Education and aged between 10 and 12 years old. The main focus of this session was to foster the development of critical cognitive and socio-emotional skills among these young learners using origami. These skills included creativity, critical analysis, mathematical reasoning, collaboration, and communication. Employing a qualitative, descriptive, and interpretative analysis of data collected during the session through field notes and students’ written productions, our findings reveal that structured origami-based activities not only promote student engagement with mathematical concepts in a playful and interactive but also facilitate the development of socio-emotional skills, which include collaboration and effective communication between participants. This research highlights the value of integrating origami into educational practices, highlighting its role in supporting comprehensive cognitive and emotional learning experiences. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=skills" title="skills">skills</a>, <a href="https://publications.waset.org/abstracts/search?q=origami%20rules" title=" origami rules"> origami rules</a>, <a href="https://publications.waset.org/abstracts/search?q=active%20learning" title=" active learning"> active learning</a>, <a href="https://publications.waset.org/abstracts/search?q=hands-on%20activities" title=" hands-on activities"> hands-on activities</a> </p> <a href="https://publications.waset.org/abstracts/172299/promoting-creative-and-critical-thinking-in-mathematics" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/172299.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">67</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2389</span> An Overview of Bioinformatics Methods to Detect Novel Riboswitches Highlighting the Importance of Structure Consideration</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Danny%20Barash">Danny Barash</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Riboswitches are RNA genetic control elements that were originally discovered in bacteria and provide a unique mechanism of gene regulation. They work without the participation of proteins and are believed to represent ancient regulatory systems in the evolutionary timescale. One of the biggest challenges in riboswitch research is that many are found in prokaryotes but only a small percentage of known riboswitches have been found in certain eukaryotic organisms. The few examples of eukaryotic riboswitches were identified using sequence-based bioinformatics search methods that include some slight structural considerations. These pattern-matching methods were the first ones to be applied for the purpose of riboswitch detection and they can also be programmed very efficiently using a data structure called affix arrays, making them suitable for genome-wide searches of riboswitch patterns. However, they are limited by their ability to detect harder to find riboswitches that deviate from the known patterns. Several methods have been developed since then to tackle this problem. The most commonly used by practitioners is Infernal that relies on Hidden Markov Models (HMMs) and Covariance Models (CMs). Profile Hidden Markov Models were also carried out in the pHMM Riboswitch Scanner web application, independently from Infernal. Other computational approaches that have been developed include RMDetect by the use of 3D structural modules and RNAbor that utilizes Boltzmann probability of structural neighbors. We have tried to incorporate more sophisticated secondary structure considerations based on RNA folding prediction using several strategies. The first idea was to utilize window-based methods in conjunction with folding predictions by energy minimization. The moving window approach is heavily geared towards secondary structure consideration relative to sequence that is treated as a constraint. However, the method cannot be used genome-wide due to its high cost because each folding prediction by energy minimization in the moving window is computationally expensive, enabling to scan only at the vicinity of genes of interest. The second idea was to remedy the inefficiency of the previous approach by constructing a pipeline that consists of inverse RNA folding considering RNA secondary structure, followed by a BLAST search that is sequence-based and highly efficient. This approach, which relies on inverse RNA folding in general and our own in-house fragment-based inverse RNA folding program called RNAfbinv in particular, shows capability to find attractive candidates that are missed by Infernal and other standard methods being used for riboswitch detection. We demonstrate attractive candidates found by both the moving-window approach and the inverse RNA folding approach performed together with BLAST. We conclude that structure-based methods like the two strategies outlined above hold considerable promise in detecting riboswitches and other conserved RNAs of functional importance in a variety of organisms. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=riboswitches" title="riboswitches">riboswitches</a>, <a href="https://publications.waset.org/abstracts/search?q=RNA%20folding%20prediction" title=" RNA folding prediction"> RNA folding prediction</a>, <a href="https://publications.waset.org/abstracts/search?q=RNA%20structure" title=" RNA structure"> RNA structure</a>, <a href="https://publications.waset.org/abstracts/search?q=structure-based%20methods" title=" structure-based methods"> structure-based methods</a> </p> <a href="https://publications.waset.org/abstracts/41500/an-overview-of-bioinformatics-methods-to-detect-novel-riboswitches-highlighting-the-importance-of-structure-consideration" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/41500.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">234</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2388</span> Effect of Electromagnetic Fields on Protein Extraction from Shrimp By-Products for Electrospinning Process</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Guido%20Trautmann-S%C3%A1ez">Guido Trautmann-Sáez</a>, <a href="https://publications.waset.org/abstracts/search?q=Mario%20P%C3%A9rez-Won"> Mario Pérez-Won</a>, <a href="https://publications.waset.org/abstracts/search?q=Vilbett%20Briones"> Vilbett Briones</a>, <a href="https://publications.waset.org/abstracts/search?q=Mar%C3%ADa%20Jos%C3%A9%20Bugue%C3%B1o"> María José Bugueño</a>, <a href="https://publications.waset.org/abstracts/search?q=Gipsy%20Tabilo-Munizaga"> Gipsy Tabilo-Munizaga</a>, <a href="https://publications.waset.org/abstracts/search?q=Luis%20Gonz%C3%A1les-Cavieres"> Luis Gonzáles-Cavieres</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Shrimp by-products are a valuable source of protein. However, traditional protein extraction methods have limitations in terms of their efficiency. Protein extraction from shrimp (Pleuroncodes monodon) industrial by-products assisted with ohmic heating (OH), microwave (MW) and pulsed electric field (PEF). It was performed by chemical method (using NaOH and HCl 2M) assisted with OH, MW and PEF in a continuous flow system (5 ml/s). Protein determination, differential scanning calorimetry (DSC) and Fourier-transform infrared (FTIR). Results indicate a 19.25% (PEF) 3.65% (OH) and 28.19% (MW) improvement in protein extraction efficiency. The most efficient method was selected for the electrospinning process and obtaining fiber. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=electrospinning%20process" title="electrospinning process">electrospinning process</a>, <a href="https://publications.waset.org/abstracts/search?q=emerging%20technology" title=" emerging technology"> emerging technology</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20extraction" title=" protein extraction"> protein extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=shrimp%20by-products" title=" shrimp by-products"> shrimp by-products</a> </p> <a href="https://publications.waset.org/abstracts/171420/effect-of-electromagnetic-fields-on-protein-extraction-from-shrimp-by-products-for-electrospinning-process" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/171420.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">89</span> </span> </div> </div> <ul class="pagination"> <li class="page-item disabled"><span class="page-link">&lsaquo;</span></li> <li class="page-item active"><span class="page-link">1</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20folding&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20folding&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20folding&page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20folding&page=5">5</a></li> <li class="page-item"><a class="page-link" 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