CINXE.COM

<!DOCTYPE html> <html lang="en" dir="ltr"> <head>  <script async src="https://www.googletagmanager.com/gtag/js?id=G-P63WKM1TM1"></script> <script> window.dataLayer = window.dataLayer || []; function gtag(){dataLayer.push(arguments);} gtag('js', new Date()); gtag('config', 'G-P63WKM1TM1'); </script>  <script type="text/javascript" > (function(m,e,t,r,i,k,a){m[i]=m[i]||function(){(m[i].a=m[i].a||[]).push(arguments)}; m[i].l=1*new Date(); for (var j = 0; j < document.scripts.length; j++) {if (document.scripts[j].src === r) { return; }} k=e.createElement(t),a=e.getElementsByTagName(t)[0],k.async=1,k.src=r,a.parentNode.insertBefore(k,a)}) (window, document, "script", "https://mc.yandex.ru/metrika/tag.js", "ym"); ym(55165297, "init", { clickmap:false, trackLinks:true, accurateTrackBounce:true, webvisor:false }); </script> <noscript><div><img src="https://mc.yandex.ru/watch/55165297" style="position:absolute; left:-9999px;" alt="" /></div></noscript>    <title>Search results for: protein masked representation</title> <meta name="description" content="Search results for: protein masked representation"> <meta name="keywords" content="protein masked representation"> <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 navbar-toggler ml-auto" type="button" data-toggle="collapse" data-target="#navbarMenu" aria-controls="navbarMenu" aria-expanded="false" aria-label="Toggle navigation"> <span class="navbar-toggler-icon"></span> </button> <div class="w-100"> <div class="d-none d-lg-flex flex-row-reverse"> <form method="get" action="https://waset.org/search" class="form-inline my-2 my-lg-0"> <input class="form-control mr-sm-2" type="search" placeholder="Search Conferences" value="protein masked representation" name="q" aria-label="Search"> <button class="btn btn-light my-2 my-sm-0" type="submit"><i class="fas fa-search"></i></button> </form> </div> <div class="collapse navbar-collapse mt-1" id="navbarMenu"> <ul class="navbar-nav ml-auto align-items-center" id="mainNavMenu"> <li class="nav-item"> <a class="nav-link" href="https://waset.org/conferences" title="Conferences in 2024/2025/2026">Conferences</a> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/disciplines" title="Disciplines">Disciplines</a> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/committees" rel="nofollow">Committees</a> </li> <li class="nav-item dropdown"> <a class="nav-link dropdown-toggle" href="#" id="navbarDropdownPublications" role="button" data-toggle="dropdown" aria-haspopup="true" aria-expanded="false"> Publications </a> <div class="dropdown-menu" aria-labelledby="navbarDropdownPublications"> <a class="dropdown-item" href="https://publications.waset.org/abstracts">Abstracts</a> <a class="dropdown-item" href="https://publications.waset.org">Periodicals</a> <a class="dropdown-item" href="https://publications.waset.org/archive">Archive</a> </div> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/page/support" title="Support">Support</a> </li> </ul> </div> </div> </nav> </div> </header> <main> <div class="container mt-4"> <div class="row"> <div class="col-md-9 mx-auto"> <form method="get" 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 masked representation"> <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> 3620</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: protein masked representation</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">3620</span> BiFormerDTA: Structural Embedding of Protein in Drug Target Affinity Prediction Using BiFormer</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Leila%20Baghaarabani">Leila Baghaarabani</a>, <a href="https://publications.waset.org/abstracts/search?q=Parvin%20Razzaghi"> Parvin Razzaghi</a>, <a href="https://publications.waset.org/abstracts/search?q=Mennatolla%20Magdy%20Mostafa"> Mennatolla Magdy Mostafa</a>, <a href="https://publications.waset.org/abstracts/search?q=Ahmad%20Albaqsami"> Ahmad Albaqsami</a>, <a href="https://publications.waset.org/abstracts/search?q=Al%20Warith%20Al%20Rushaidi"> Al Warith Al Rushaidi</a>, <a href="https://publications.waset.org/abstracts/search?q=Masoud%20Al%20Rawahi"> Masoud Al Rawahi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Predicting the interaction between drugs and their molecular targets is pivotal for advancing drug development processes. Due to the time and cost limitations, computational approaches have emerged as an effective approach to drug-target interaction (DTI) prediction. Most of the introduced computational based approaches utilize the drug molecule and protein sequence as input. This study does not only utilize these inputs, it also introduces a protein representation developed using a masked protein language model. In this representation, for every individual amino acid residue within the protein sequence, there exists a corresponding probability distribution that indicates the likelihood of each amino acid being present at that particular position. Then, the similarity between each pair of amino acids is computed to create a similarity matrix. To encode the knowledge of the similarity matrix, Bi-Level Routing Attention (BiFormer) is utilized, which combines aspects of transformer-based models with protein sequence analysis and represents a significant advancement in the field of drug-protein interaction prediction. BiFormer has the ability to pinpoint the most effective regions of the protein sequence that are responsible for facilitating interactions between the protein and drugs, thereby enhancing the understanding of these critical interactions. Thus, it appears promising in its ability to capture the local structural relationship of the proteins by enhancing the understanding of how it contributes to drugprotein interactions, thereby facilitating more accurate predictions. To evaluate the proposed method, it was tested on two widely recognized datasets: Davis and KIBA. A comprehensive series of experiments was conducted to illustrate its effectiveness in comparison to cutting edge techniques. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=BiFormer" title="BiFormer">BiFormer</a>, <a href="https://publications.waset.org/abstracts/search?q=transformer" title=" transformer"> transformer</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20language%20processing" title=" protein language processing"> protein language processing</a>, <a href="https://publications.waset.org/abstracts/search?q=self-attention%20mechanism" title=" self-attention mechanism"> self-attention mechanism</a>, <a href="https://publications.waset.org/abstracts/search?q=binding%20affinity" title=" binding affinity"> binding affinity</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20target%20interaction" title=" drug target interaction"> drug target interaction</a>, <a href="https://publications.waset.org/abstracts/search?q=similarity%20matrix" title=" similarity matrix"> similarity matrix</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation" title=" protein masked representation"> protein masked representation</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20language%20model" title=" protein language model"> protein language model</a> </p> <a href="https://publications.waset.org/abstracts/194594/biformerdta-structural-embedding-of-protein-in-drug-target-affinity-prediction-using-biformer" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/194594.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">7</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">3619</span> Masked Candlestick Model: A Pre-Trained Model for Trading Prediction</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ling%20Qi">Ling Qi</a>, <a href="https://publications.waset.org/abstracts/search?q=Matloob%20Khushi"> Matloob Khushi</a>, <a href="https://publications.waset.org/abstracts/search?q=Josiah%20Poon"> Josiah Poon</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This paper introduces a pre-trained Masked Candlestick Model (MCM) for trading time-series data. The pre-trained model is based on three core designs. First, we convert trading price data at each data point as a set of normalized elements and produce embeddings of each element. Second, we generate a masked sequence of such embedded elements as inputs for self-supervised learning. Third, we use the encoder mechanism from the transformer to train the inputs. The masked model learns the contextual relations among the sequence of embedded elements, which can aid downstream classification tasks. To evaluate the performance of the pre-trained model, we fine-tune MCM for three different downstream classification tasks to predict future price trends. The fine-tuned models achieved better accuracy rates for all three tasks than the baseline models. To better analyze the effectiveness of MCM, we test the same architecture for three currency pairs, namely EUR/GBP, AUD/USD, and EUR/JPY. The experimentation results demonstrate MCM’s effectiveness on all three currency pairs and indicate the MCM’s capability for signal extraction from trading data. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=masked%20language%20model" title="masked language model">masked language model</a>, <a href="https://publications.waset.org/abstracts/search?q=transformer" title=" transformer"> transformer</a>, <a href="https://publications.waset.org/abstracts/search?q=time%20series%20prediction" title=" time series prediction"> time series prediction</a>, <a href="https://publications.waset.org/abstracts/search?q=trading%20prediction" title=" trading prediction"> trading prediction</a>, <a href="https://publications.waset.org/abstracts/search?q=embedding" title=" embedding"> embedding</a>, <a href="https://publications.waset.org/abstracts/search?q=transfer%20learning" title=" transfer learning"> transfer learning</a>, <a href="https://publications.waset.org/abstracts/search?q=self-supervised%20learning" title=" self-supervised learning"> self-supervised learning</a> </p> <a href="https://publications.waset.org/abstracts/153348/masked-candlestick-model-a-pre-trained-model-for-trading-prediction" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/153348.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">126</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">3618</span> Transfer Learning for Protein Structure Classification at Low Resolution</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alexander%20Hudson">Alexander Hudson</a>, <a href="https://publications.waset.org/abstracts/search?q=Shaogang%20Gong"> Shaogang Gong</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Structure determination is key to understanding protein function at a molecular level. Whilst significant advances have been made in predicting structure and function from amino acid sequence, researchers must still rely on expensive, time-consuming analytical methods to visualise detailed protein conformation. In this study, we demonstrate that it is possible to make accurate (≥80%) predictions of protein class and architecture from structures determined at low (>3A) resolution, using a deep convolutional neural network trained on high-resolution (≤3A) structures represented as 2D matrices. Thus, we provide proof of concept for high-speed, low-cost protein structure classification at low resolution, and a basis for extension to prediction of function. We investigate the impact of the input representation on classification performance, showing that side-chain information may not be necessary for fine-grained structure predictions. Finally, we confirm that high resolution, low-resolution and NMR-determined structures inhabit a common feature space, and thus provide a theoretical foundation for boosting with single-image super-resolution. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=transfer%20learning" title="transfer learning">transfer learning</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20distance%20maps" title=" protein distance maps"> protein distance maps</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20structure%20classification" title=" protein structure classification"> protein structure classification</a>, <a href="https://publications.waset.org/abstracts/search?q=neural%20networks" title=" neural networks"> neural networks</a> </p> <a href="https://publications.waset.org/abstracts/129704/transfer-learning-for-protein-structure-classification-at-low-resolution" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/129704.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">136</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">3617</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">3616</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">3615</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">3614</span> The Representation of J. D. Salinger’s Views on Changes in American Society in the 1940s in The Catcher in the Rye</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jessadaporn%20Achariyopas">Jessadaporn Achariyopas</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The objectives of this study aim to analyze both the protagonist in The Catcher in the Rye in terms of ideological concepts and narrative techniques which influence the construction of the representation and the relationship between the representation and J. D. Salinger’s views on changes in American society in the 1940s. This area of study might concern two theories: namely, a theory of representation and narratology. In addition, this research is intended to answer the following three questions. Firstly, how is the production of meaning through language in The Catcher in the Rye constructed? Secondly, what are J. D. Salinger’s views on changes in American society in the 1940s? Lastly, how is the relationship between the representation and J. D. Salinger’s views? The findings showed that the protagonist’s views, J. D. Salinger’s views, and changes in American society in the 1940s are obviously interrelated. The production of meaning which is the representation of the protagonist’s views was constructed of narrative techniques. J. D. Salinger’s views on changes in American society in the 1940s were the same antisocial perspectives as Holden Caulfield’s which are phoniness, alienation and meltdown. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=representation" title="representation">representation</a>, <a href="https://publications.waset.org/abstracts/search?q=construction%20of%20the%20representation" title=" construction of the representation"> construction of the representation</a>, <a href="https://publications.waset.org/abstracts/search?q=systems%20of%20representation" title=" systems of representation"> systems of representation</a>, <a href="https://publications.waset.org/abstracts/search?q=phoniness" title=" phoniness"> phoniness</a>, <a href="https://publications.waset.org/abstracts/search?q=alienation" title=" alienation"> alienation</a>, <a href="https://publications.waset.org/abstracts/search?q=meltdown" title=" meltdown"> meltdown</a> </p> <a href="https://publications.waset.org/abstracts/9035/the-representation-of-j-d-salingers-views-on-changes-in-american-society-in-the-1940s-in-the-catcher-in-the-rye" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/9035.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">321</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">3613</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">3612</span> Innovative Pictogram Chinese Characters Representation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=J.%20H.%20Low">J. H. Low</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20H.%20Hew"> S. H. Hew</a>, <a href="https://publications.waset.org/abstracts/search?q=C.%20O.%20Wong"> C. O. Wong</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This paper proposes an innovative approach to represent the pictogram Chinese characters. The advantage of this representation is using an extraordinary to represent the pictogram Chinese character. This extraordinary representation is created accordingly to the original pictogram Chinese characters revolution. The purpose of this innovative creation is to assistant the learner learning Chinese as second language (SCL) in Chinese language learning specifically on memorize Chinese characters. Commonly, the SCL will give up and frustrate easily while memorize the Chinese characters by rote. So, our innovative representation is able to help on memorize the Chinese character by the help of visually storytelling. This innovative representation enhances the Chinese language learning experience of SCL. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Chinese%20e-learning" title="Chinese e-learning">Chinese e-learning</a>, <a href="https://publications.waset.org/abstracts/search?q=innovative%20Chinese%20character%20representation" title=" innovative Chinese character representation"> innovative Chinese character representation</a>, <a href="https://publications.waset.org/abstracts/search?q=knowledge%20management" title=" knowledge management"> knowledge management</a>, <a href="https://publications.waset.org/abstracts/search?q=language%20learning" title=" language learning"> language learning</a> </p> <a href="https://publications.waset.org/abstracts/4346/innovative-pictogram-chinese-characters-representation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/4346.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">487</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">3611</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">3610</span> Elucidating the Genetic Determinism of Seed Protein Plasticity in Response to the Environment Using Medicago truncatula</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=K.%20Cartelier">K. Cartelier</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20Aime"> D. Aime</a>, <a href="https://publications.waset.org/abstracts/search?q=V.%20Vernoud"> V. Vernoud</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Buitink"> J. Buitink</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20M.%20Prosperi"> J. M. Prosperi</a>, <a href="https://publications.waset.org/abstracts/search?q=K.%20Gallardo"> K. Gallardo</a>, <a href="https://publications.waset.org/abstracts/search?q=C.%20Le%20Signor"> C. Le Signor</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Legumes can produce protein-rich seeds without nitrogen fertilizer through root symbiosis with nitrogen-fixing rhizobia. Rich in lysine, these proteins are used for human nutrition and animal feed. However, the instability of seed protein yield and quality due to environmental fluctuations limits the wider use of legumes such as pea. Breeding efforts are needed to optimize and stabilize seed nutritional value, which requires to identify the genetic determinism of seed protein plasticity in response to the environment. Towards this goal, we have studied the plasticity of protein content and composition of seeds from a collection of 200 Medicago truncatula ecotypes grown under four controlled conditions (optimal, drought, and winter/spring sowing). A quantitative analysis of one-dimensional protein profiles of these mature seeds was performed and plasticity indices were calculated from each abundant protein band. Genome-Wide Association Studies (GWAS) from these data identified major GWAS hotspots, from which a list of candidate genes was obtained. A Gene Ontology Enrichment Analysis revealed an over-representation of genes involved in several amino acid metabolic pathways. This led us to propose that environmental variations are likely to modulate amino acid balance, thus impacting seed protein composition. The selection of candidate genes for controlling the plasticity of seed protein composition was refined using transcriptomics data from developing Medicago truncatula seeds. The pea orthologs of key genes were identified for functional studies by mean of TILLING (Targeting Induced Local Lesions in Genomes) lines in this crop. We will present how this study highlighted mechanisms that could govern seed protein plasticity, providing new cues towards the stabilization of legume seed quality. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=GWAS" title="GWAS">GWAS</a>, <a href="https://publications.waset.org/abstracts/search?q=Medicago%20truncatula" title=" Medicago truncatula"> Medicago truncatula</a>, <a href="https://publications.waset.org/abstracts/search?q=plasticity" title=" plasticity"> plasticity</a>, <a href="https://publications.waset.org/abstracts/search?q=seed" title=" seed"> seed</a>, <a href="https://publications.waset.org/abstracts/search?q=storage%20proteins" title=" storage proteins"> storage proteins</a> </p> <a href="https://publications.waset.org/abstracts/114311/elucidating-the-genetic-determinism-of-seed-protein-plasticity-in-response-to-the-environment-using-medicago-truncatula" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/114311.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">142</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">3609</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> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">3608</span> Physicochemical Properties of Soy Protein Isolate (SPI): Starch Conjugates Treated by Sonication</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gulcin%20Yildiz">Gulcin Yildiz</a>, <a href="https://publications.waset.org/abstracts/search?q=Hao%20Feng"> Hao Feng</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In recent years there is growing interested in using soy protein because of several advantages compared to other protein sources, such as high nutritional value, steady supply, and low cost. Soy protein isolate (SPI) is the most refined soy protein product. It contains 90% protein in a moisture-free form and has some desirable functionalities. Creating a protein-polysaccharide conjugate to be the emulsifying agent rather than the protein alone can markedly enhance its stability. This study was undertaken to examine the effects of ultrasound treatments on the physicochemical properties of SPI-starch conjugates. The soy protein isolate (SPI, Pro-Fam® 955) samples were obtained from the Archer Daniels Midland Company. Protein concentrations were analyzed by the Bardford method using BSA as the standard. The volume-weighted mean diameters D [4,3] of protein–polysaccharide conjugates were measured by dynamic light scattering (DLS). Surface hydrophobicity of the conjugates was measured by using 1-anilino-8-naphthalenesulfonate (ANS) (Sigma-Aldrich, St. Louis, MO, USA). Increasing the pH from 2 to 12 resulted in increased protein solubility. The highest solubility was 69.2% for the sample treated with ultrasonication at pH 12, while the lowest (9.13%) was observed in the Control. For the other pH conditions, the protein solubility values ranged from 40.53 to 49.65%. The ultrasound treatment significantly decreased the particle sizes of the SPI-modified starch conjugates. While the D [4,3] for the Control was 731.6 nm, it was 293.7 nm for the samples treated by sonication at pH 12. The surface hydrophobicity (H0) of SPI-starch at all pH conditions were significantly higher than those in the Control. Ultrasonication was proven to be effective in improving the solubility and emulsifying properties of soy protein isolate-starch conjugates. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=particle%20size" title="particle size">particle size</a>, <a href="https://publications.waset.org/abstracts/search?q=solubility" title=" solubility"> solubility</a>, <a href="https://publications.waset.org/abstracts/search?q=soy%20protein%20isolate" title=" soy protein isolate"> soy protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=ultrasonication" title=" ultrasonication"> ultrasonication</a> </p> <a href="https://publications.waset.org/abstracts/64023/physicochemical-properties-of-soy-protein-isolate-spi-starch-conjugates-treated-by-sonication" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/64023.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">422</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">3607</span> Effect of Removing Hub Domain on Human CaMKII Isoforms Sensitivity to Calcium/Calmodulin</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ravid%20Inbar">Ravid Inbar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> CaMKII (calcium-calmodulin dependent protein kinase II) makes up 2% of the protein in our brain and has a critical role in memory formation and long-term potentiation of neurons. Despite this, research has yet to uncover the role of one of the domains on the activation of this kinase. The following proposes to express the protein without the hub domain in E. coli, leaving only the kinase and regulatory segment of the protein. Next, a series of kinase assays will be conducted to elucidate the role the hub domain plays on CaMKII sensitivity to calcium/calmodulin activation. The hub domain may be important for activation; however, it may also be a variety of domains working together to influence protein activation and not the hub alone. Characterization of a protein is critical to the future understanding of the protein's function, as well as for producing pharmacological targets in cases of patients with diseases. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=CaMKII" title="CaMKII">CaMKII</a>, <a href="https://publications.waset.org/abstracts/search?q=hub%20domain" title=" hub domain"> hub domain</a>, <a href="https://publications.waset.org/abstracts/search?q=kinase%20assays" title=" kinase assays"> kinase assays</a>, <a href="https://publications.waset.org/abstracts/search?q=kinase%20%2B%20reg%20seg" title=" kinase + reg seg"> kinase + reg seg</a> </p> <a href="https://publications.waset.org/abstracts/157748/effect-of-removing-hub-domain-on-human-camkii-isoforms-sensitivity-to-calciumcalmodulin" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/157748.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> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">3606</span> Fortification of Concentrated Milk Protein Beverages with Soy Proteins: Impact of Divalent Cations and Heating Treatment on the Physical Stability</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Yichao%20Liang">Yichao Liang</a>, <a href="https://publications.waset.org/abstracts/search?q=Biye%20Chen"> Biye Chen</a>, <a href="https://publications.waset.org/abstracts/search?q=Xiang%20Li"> Xiang Li</a>, <a href="https://publications.waset.org/abstracts/search?q=Steven%20R.%20Dimler"> Steven R. Dimler</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study investigated the effects of adding calcium and magnesium chloride on heat and storage stability of milk protein concentrate-soy protein isolate (8:2 respectively) mixtures containing 10% w/w total protein subjected to the in-container sterilization (115 °C x 15 min). The particle size does not change when emulsions are heated at pH between 6.7 and 7.3 irrespective of the mixed protein ratio. Increasing concentration of divalent cation salts resulted in an increase in protein particle size, dry sediment formation and sediment height and a decrease in pH, heat stability and hydration in milk protein concentrate-soy protein isolate mixtures solutions on sterilization at 115°C. Fortification of divalent cation salts in milk protein concentrate-soy protein isolate mixture solutions resulted in an accelerated protein sedimentation and two unique sediment regions during accelerated storage stability testing. Moreover, the heat stability decreased upon sterilization at 115°C, with addition of MgCl₂ causing a greater increase in sedimentation velocity and compressibility than CaCl₂. Increasing pH value of protein milk concentrate-soy protein isolate mixtures solutions from 6.7 to 7.2 resulted in an increase in viscosity following the heat treatment. The study demonstrated that the type and concentration of divalent cation salts used strongly impact heat and storage stability of milk protein concentrate-soy protein isolate mixture nutritional beverages. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=divalent%20cation%20salts" title="divalent cation salts">divalent cation salts</a>, <a href="https://publications.waset.org/abstracts/search?q=heat%20stability" title=" heat stability"> heat stability</a>, <a href="https://publications.waset.org/abstracts/search?q=milk%20protein%20concentrate" title=" milk protein concentrate"> milk protein concentrate</a>, <a href="https://publications.waset.org/abstracts/search?q=soy%20protein%20isolate" title=" soy protein isolate"> soy protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=storage%20stability" title=" storage stability"> storage stability</a> </p> <a href="https://publications.waset.org/abstracts/94469/fortification-of-concentrated-milk-protein-beverages-with-soy-proteins-impact-of-divalent-cations-and-heating-treatment-on-the-physical-stability" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/94469.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">331</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">3605</span> The Relation Between Protein-Protein and Polysaccharide-Protein Interaction on Aroma Release from Brined Cheese Model</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mehrnaz%20Aminifar">Mehrnaz Aminifar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The relation between textural parameters and casein network on release of aromatic compounds was investigated over 90-days of ripening. Low DE maltodextrin and WPI were used to modify the textural properties of low fat brined cheese. Hardness, brittleness and compaction of casein network were affected by addition of maltodextrin and WPI. Textural properties and aroma release from cheese texture were affected by interaction of WPI protein-cheese protein and maltodexterin-cheese protein. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aroma%20release" title="aroma release">aroma release</a>, <a href="https://publications.waset.org/abstracts/search?q=brined%20cheese" title=" brined cheese"> brined cheese</a>, <a href="https://publications.waset.org/abstracts/search?q=maltodexterin" title=" maltodexterin"> maltodexterin</a>, <a href="https://publications.waset.org/abstracts/search?q=WPI" title=" WPI"> WPI</a> </p> <a href="https://publications.waset.org/abstracts/6193/the-relation-between-protein-protein-and-polysaccharide-protein-interaction-on-aroma-release-from-brined-cheese-model" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/6193.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">354</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">3604</span> Amino Acid Profile, Protein Digestibility, Antioxidant and Functional Properties of Protein Concentrate of Local Varieties (Kwandala, Yardass, Jeep, and Jamila) of Rice Brands from Nigeria</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=C.%20E.%20Chinma">C. E. Chinma</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20O.%20Azeez"> S. O. Azeez</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20C.%20Anuonye"> J. C. Anuonye</a>, <a href="https://publications.waset.org/abstracts/search?q=O.%20B.%20Ocheme"> O. B. Ocheme</a>, <a href="https://publications.waset.org/abstracts/search?q=C.%20M.%20Yakubu"> C. M. Yakubu</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20James"> S. James</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20U.%20Ohuoba"> E. U. Ohuoba</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20A.%20Baba"> I. A. Baba </a> </p> <p class="card-text"><strong>Abstract:</strong></p> There is growing interest in the use of rice bran protein in food formulation due to its hypoallergenic protein, high nutritional value and health promoting potentials. For the first time, the amino acid profile, protein digestibility, antioxidant, and functional properties of protein concentrate from some local varieties of rice bran from Nigeria were studied for possible food applications. Protein concentrates were prepared from rice bran and analysed using standard methods. Results showed that protein content of Kwandala, Yardass, Jeep, and Jamila were 69.24%, 69.97%, 68.73%, and 71.62%, respectively while total essential amino acid were 52.71, 53.03, 51.86, and 55.75g/100g protein, respectively. In vitro protein digestibility of protein concentrate from Kwandala, Yardass, Jeep and Jamila were 90.70%, 91.39%, 90.57% and 91.63% respectively. DPPH radical inhibition of protein from Kwandala, Yardass, Jeep, and Jamila were 48.15%, 48.90%, 47.56%, and 53.29%, respectively while ferric reducing ability power were 0.52, 0.55, 0.47 and 0.67mmol TE per gram, respectively. Protein concentrate from Jamila had higher onset (92.57oC) and denaturation temperature (102.13oC), and enthalpy (0.72J/g) than Jeep (91.46oC, 101.76oC, and 0.68J/g, respectively), Kwandala (90.32oC, 100.54oC and 0.57J/g, respectively), and Yardass (88.94oC, 99.45oC, and 0.51J/g, respectively). In vitro digestibility of protein from Kwandala, Yardas, Jeep, and Jamila were 90.70%, 91.39%, 90.57% and 91.63% respectively. Oil absorption capacity of Kwandala, Yardass, Jeep, and Jamila were 3.61, 3.73, 3.40, and 4.23g oil/g sample respectively, while water absorption capacity were 4.19, 4.32, 3.55 and 4.48g water/g sample, respectively. Protein concentrates had low bulk density (0.37-0.43g/ml). Protein concentrate from Jamila rice bran had the highest foam capacity (37.25%), followed by Yardass (34.20%), Kwandala (30.14%) and Jeep (28.90%). Protein concentrates showed low emulsifying and gelling capacities. In conclusion, protein concentrate prepared from these local rice bran varieties could serve as functional ingredients in food formulations and for enriching low protein foods. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=rice%20bran%20protein" title="rice bran protein">rice bran protein</a>, <a href="https://publications.waset.org/abstracts/search?q=amino%20acid%20profile" title=" amino acid profile"> amino acid profile</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20digestibility" title=" protein digestibility"> protein digestibility</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20and%20functional%20properties" title=" antioxidant and functional properties"> antioxidant and functional properties</a> </p> <a href="https://publications.waset.org/abstracts/17730/amino-acid-profile-protein-digestibility-antioxidant-and-functional-properties-of-protein-concentrate-of-local-varieties-kwandala-yardass-jeep-and-jamila-of-rice-brands-from-nigeria" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/17730.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">370</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">3603</span> Analysis of Formyl Peptide Receptor 1 Protein Value as an Indicator of Neutrophil Chemotaxis Dysfunction in Aggressive Periodontitis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Prajna%20Metta">Prajna Metta</a>, <a href="https://publications.waset.org/abstracts/search?q=Yanti%20Rusyanti"> Yanti Rusyanti</a>, <a href="https://publications.waset.org/abstracts/search?q=Nunung%20Rusminah"> Nunung Rusminah</a>, <a href="https://publications.waset.org/abstracts/search?q=Bremmy%20Laksono"> Bremmy Laksono</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The decrease of neutrophil chemotaxis function may cause increased susceptibility to aggressive periodontitis (AP). Neutrophil chemotaxis is affected by formyl peptide receptor 1 (FPR1), which when activated will respond to bacterial chemotactic peptide formyl methionyl leusyl phenylalanine (FMLP). FPR1 protein value is decreased in response to a wide number of inflammatory stimuli in AP patients. This study was aimed to assess the alteration of FPR1 protein value in AP patients and if FPR1 protein value could be used as an indicator of neutrophil chemotaxis dysfunction in AP. This is a case control study with 20 AP patients and 20 control subjects. Three milliliters of peripheral blood were drawn and analyzed for FPR1 protein value with ELISA. The data were statistically analyzed with Mann-Whitney test (p>0,05<u>)</u>. Results showed that the mean value of FPR1 protein value in AP group is 0,353 pg/mL (0,11 to 1,18 pg/mL) and the mean value of FPR1 protein value in control group is 0,296 pg/mL (0,05 to 0,88 pg/mL). P value 0,787 > 0,05 suggested that there is no significant difference of FPR1 protein value in both groups. The present study suggests that FPR1 protein value has no significance alteration in AP patients and could not be used as an indicator of neutrophil chemotaxis dysfunction. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aggressive%20periodontitis" title="aggressive periodontitis">aggressive periodontitis</a>, <a href="https://publications.waset.org/abstracts/search?q=chemotaxis%20dysfunction" title=" chemotaxis dysfunction"> chemotaxis dysfunction</a>, <a href="https://publications.waset.org/abstracts/search?q=FPR1%20protein%20value" title=" FPR1 protein value"> FPR1 protein value</a>, <a href="https://publications.waset.org/abstracts/search?q=neutrophil" title=" neutrophil"> neutrophil</a> </p> <a href="https://publications.waset.org/abstracts/58541/analysis-of-formyl-peptide-receptor-1-protein-value-as-an-indicator-of-neutrophil-chemotaxis-dysfunction-in-aggressive-periodontitis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/58541.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">217</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">3602</span> Selection of Pichia kudriavzevii Strain for the Production of Single-Cell Protein from Cassava Processing Waste</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Phakamas%20Rachamontree">Phakamas Rachamontree</a>, <a href="https://publications.waset.org/abstracts/search?q=Theerawut%20Phusantisampan"> Theerawut Phusantisampan</a>, <a href="https://publications.waset.org/abstracts/search?q=Natthakorn%20Woravutthikul"> Natthakorn Woravutthikul</a>, <a href="https://publications.waset.org/abstracts/search?q=Peerapong%20Pornwongthong"> Peerapong Pornwongthong</a>, <a href="https://publications.waset.org/abstracts/search?q=Malinee%20Sriariyanun"> Malinee Sriariyanun</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A total of 115 yeast strains isolated from local cassava processing wastes were measured for crude protein content. Among these strains, the strain MSY-2 possessed the highest protein concentration (>3.5 mg protein/mL). By using molecular identification tools, it was identified to be a strain of Pichia kudriavzevii based on similarity of D1/D2 domain of 26S rDNA region. In this study, to optimize the protein production by MSY-2 strain, Response Surface Methodology (RSM) was applied. The tested parameters were the carbon content, nitrogen content, and incubation time. Here, the value of regression coefficient (R2) = 0.7194 could be explained by the model, which is high to support the significance of the model. Under the optimal condition, the protein content was produced up to 3.77 g per L of the culture and MSY-2 strain contain 66.8 g protein per 100 g of cell dry weight. These results revealed the plausibility of applying the novel strain of yeast in single-cell protein production. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=single%20cell%20protein" title="single cell protein">single cell protein</a>, <a href="https://publications.waset.org/abstracts/search?q=response%20surface%20methodology" title=" response surface methodology"> response surface methodology</a>, <a href="https://publications.waset.org/abstracts/search?q=yeast" title=" yeast"> yeast</a>, <a href="https://publications.waset.org/abstracts/search?q=cassava%20processing%20waste" title=" cassava processing waste"> cassava processing waste</a> </p> <a href="https://publications.waset.org/abstracts/27179/selection-of-pichia-kudriavzevii-strain-for-the-production-of-single-cell-protein-from-cassava-processing-waste" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/27179.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">402</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">3601</span> Effect of Different Irrigation Intervals on Protein and Gel Production of Aloe Vera (Aloe Barbadensis M.) in Iran</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Seyed%20Mohammad%20Hosein%20Al%20Omrani%20Nejad">Seyed Mohammad Hosein Al Omrani Nejad</a>, <a href="https://publications.waset.org/abstracts/search?q=Ali%20Rezvani%20Aghdam"> Ali Rezvani Aghdam</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study was done in order to evaluation different irrigation intervals on amount of protein, and gel production in Aloe vera, a traditional medicinal plant. Plants was plnted in Greenhouse and irrigated according to Accumulative Pan Evaporation(APE). The treatments were included 20, 40, 60, 80, 100, 120, 140, 160, 180, and 200 mm APE which has been showed W1,W2, W3, W4, W5, W6, W7, W8,W9 and W10 respectively.The amount of protein and gel production was measured seperately. Results showed that highest protein and fresh weight of gel obtained plants which irrigated W6 and W7 respectively. According to these results can recomend which if plant irrigatedwhen APE reached 120 and 140 mm by Class A Evaporation Pan method gel production and protein would besuitable in north of khozestan province in limited irrigation conditions. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=irrigation" title="irrigation">irrigation</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=gel" title=" gel"> gel</a>, <a href="https://publications.waset.org/abstracts/search?q=aloe%20vera" title=" aloe vera"> aloe vera</a>, <a href="https://publications.waset.org/abstracts/search?q=Iran" title=" Iran"> Iran</a> </p> <a href="https://publications.waset.org/abstracts/30907/effect-of-different-irrigation-intervals-on-protein-and-gel-production-of-aloe-vera-aloe-barbadensis-m-in-iran" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/30907.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">389</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">3600</span> Bio-Functional Polymeric Protein Based Materials Utilized for Soft Tissue Engineering Application </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Er-Yuan%20Chuang">Er-Yuan Chuang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Bio-mimetic matters have biological functionalities. This might be valuable in the development of versatile biomaterials. At biological fields, protein-based materials might be components to form a 3D network of extracellular biomolecules, containing growth factors. Also, the protein-based biomaterial provides biochemical and structural assistance of adjacent cells. In this study, we try to prepare protein based biomaterial, which was harvested from living animal. We analyzed it’s chemical, physical and biological property in vitro. Besides, in vivo bio-interaction of the prepared biomimetic matrix was tested in an animal model. The protein-based biomaterial has degradability and biocompatibility. This development could be used for tissue regenerations and be served as platform technologies. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20based" title="protein based">protein based</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vitro%20study" title=" in vitro study"> in vitro study</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vivo%20study" title=" in vivo study"> in vivo study</a>, <a href="https://publications.waset.org/abstracts/search?q=biomaterials" title=" biomaterials"> biomaterials</a> </p> <a href="https://publications.waset.org/abstracts/105449/bio-functional-polymeric-protein-based-materials-utilized-for-soft-tissue-engineering-application" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/105449.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">189</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">3599</span> Protein Isolates from Chickpea (Cicer arietinum L.) and Its Application in Cake</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohamed%20Abdullah%20Ahmed">Mohamed Abdullah Ahmed</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In a study of chickpea protein isolate (CPI) preparation, the wet alkaline extraction was carried out. The objectives were to determine the optimal extracting conditions of CPI and apply CPI into a sponge cake recipe to replace egg and make acceptable product. The design used in extraction was a central composite design. The response surface methodology was preferred to graphically express the relationship between extraction time and pH with the output variables of percent yield and protein content of CPI. It was noted that optimal extracting conditions were 60 min and pH 10.5 resulting in 90.07% protein content and 89.15% yield of CPI. The protein isolate (CPI) could be incorporated in cake to 20% without adversely affecting the cake physical properties such as cake hardness and sensory attributes. The higher protein content in cake was corresponding to the amount of CPI added. Therefore, adding CPI can significantly (p<0.05) increase protein content in cake. However, sensory evaluation showed that adding more than 20% of CPI decreased the overall acceptability. The results of this investigation could be used as a basic knowledge of CPI utilization in other food products. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chick%20bean%20protein%20isolate" title="chick bean protein isolate">chick bean protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=sponge%20cake" title=" sponge cake"> sponge cake</a>, <a href="https://publications.waset.org/abstracts/search?q=utilization" title=" utilization"> utilization</a>, <a href="https://publications.waset.org/abstracts/search?q=sponge" title=" sponge "> sponge </a> </p> <a href="https://publications.waset.org/abstracts/10335/protein-isolates-from-chickpea-cicer-arietinum-l-and-its-application-in-cake" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/10335.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">366</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">3598</span> Constructing White-Box Implementations Based on Threshold Shares and Composite Fields</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tingting%20%20Lin">Tingting Lin</a>, <a href="https://publications.waset.org/abstracts/search?q=Manfred%20von%20Willich"> Manfred von Willich</a>, <a href="https://publications.waset.org/abstracts/search?q=Dafu%20Lou"> Dafu Lou</a>, <a href="https://publications.waset.org/abstracts/search?q=Phil%20Eisen"> Phil Eisen</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A white-box implementation of a cryptographic algorithm is a software implementation intended to resist extraction of the secret key by an adversary. To date, most of the white-box techniques are used to protect block cipher implementations. However, a large proportion of the white-box implementations are proven to be vulnerable to affine equivalence attacks and other algebraic attacks, as well as differential computation analysis (DCA). In this paper, we identify a class of block ciphers for which we propose a method of constructing white-box implementations. Our method is based on threshold implementations and operations in composite fields. The resulting implementations consist of lookup tables and few exclusive OR operations. All intermediate values (inputs and outputs of the lookup tables) are masked. The threshold implementation makes the distribution of the masked values uniform and independent of the original inputs, and the operations in composite fields reduce the size of the lookup tables. The white-box implementations can provide resistance against algebraic attacks and DCA-like attacks. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=white-box" title="white-box">white-box</a>, <a href="https://publications.waset.org/abstracts/search?q=block%20cipher" title=" block cipher"> block cipher</a>, <a href="https://publications.waset.org/abstracts/search?q=composite%20field" title=" composite field"> composite field</a>, <a href="https://publications.waset.org/abstracts/search?q=threshold%20implementation" title=" threshold implementation"> threshold implementation</a> </p> <a href="https://publications.waset.org/abstracts/108457/constructing-white-box-implementations-based-on-threshold-shares-and-composite-fields" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/108457.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">168</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">3597</span> Non Commutative Lᵖ Spaces as Hilbert Modules</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Salvatore%20Triolo">Salvatore Triolo</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We discuss the possibility of extending the well-known Gelfand-Naimark-Segal representation to modules over a C*algebra. We focus our attention on the case of Hilbert modules. We consider, in particular, the problem of the existence of a faithful representation. Non-commutative Lᵖ-spaces are shown to constitute examples of a class of CQ*-algebras. Finally, we have shown that any semisimple proper CQ*-algebra (X, A#), with A# a W*-algebra can be represented as a CQ*-algebra of measurable operators in Segal’s sense. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gelfand-Naimark-Segal%20representation" title="Gelfand-Naimark-Segal representation">Gelfand-Naimark-Segal representation</a>, <a href="https://publications.waset.org/abstracts/search?q=CQ%2A-algebras" title=" CQ*-algebras"> CQ*-algebras</a>, <a href="https://publications.waset.org/abstracts/search?q=faithful%20representation" title=" faithful representation"> faithful representation</a>, <a href="https://publications.waset.org/abstracts/search?q=non-commutative%20L%E1%B5%96-spaces" title=" non-commutative Lᵖ-spaces"> non-commutative Lᵖ-spaces</a>, <a href="https://publications.waset.org/abstracts/search?q=operator%20in%20Hilbert%20spaces" title=" operator in Hilbert spaces"> operator in Hilbert spaces</a> </p> <a href="https://publications.waset.org/abstracts/142662/non-commutative-l-spaces-as-hilbert-modules" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/142662.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">248</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">3596</span> Combining in vitro Protein Expression with AlphaLISA Technology to Study Protein-Protein Interaction</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shayli%20Varasteh%20Moradi">Shayli Varasteh Moradi</a>, <a href="https://publications.waset.org/abstracts/search?q=Wayne%20A.%20Johnston"> Wayne A. Johnston</a>, <a href="https://publications.waset.org/abstracts/search?q=Dejan%20Gagoski"> Dejan Gagoski</a>, <a href="https://publications.waset.org/abstracts/search?q=Kirill%20Alexandrov"> Kirill Alexandrov</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The demand for a rapid and more efficient technique to identify protein-protein interaction particularly in the areas of therapeutics and diagnostics development is growing. The method described here is a rapid in vitro protein-protein interaction analysis approach based on AlphaLISA technology combined with Leishmania tarentolae cell-free protein production (LTE) system. Cell-free protein synthesis allows the rapid production of recombinant proteins in a multiplexed format. Among available in vitro expression systems, LTE offers several advantages over other eukaryotic cell-free systems. It is based on a fast growing fermentable organism that is inexpensive in cultivation and lysate production. High integrity of proteins produced in this system and the ability to co-express multiple proteins makes it a desirable method for screening protein interactions. Following the translation of protein pairs in LTE system, the physical interaction between proteins of interests is analysed by AlphaLISA assay. The assay is performed using unpurified in vitro translation reaction and therefore can be readily multiplexed. This approach can be used in various research applications such as epitope mapping, antigen-antibody analysis and protein interaction network mapping. The intra-viral protein interaction network of Zika virus was studied using the developed technique. The viral proteins were co-expressed pair-wise in LTE and all possible interactions among viral proteins were tested using AlphaLISA. The assay resulted to the identification of 54 intra-viral protein-protein interactions from which 19 binary interactions were found to be novel. The presented technique provides a powerful tool for rapid analysis of protein-protein interaction with high sensitivity and throughput. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=AlphaLISA%20technology" title="AlphaLISA technology">AlphaLISA technology</a>, <a href="https://publications.waset.org/abstracts/search?q=cell-free%20protein%20expression" title=" cell-free protein expression"> cell-free protein expression</a>, <a href="https://publications.waset.org/abstracts/search?q=epitope%20mapping" title=" epitope mapping"> epitope mapping</a>, <a href="https://publications.waset.org/abstracts/search?q=Leishmania%20tarentolae" title=" Leishmania tarentolae"> Leishmania tarentolae</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-protein%20interaction" title=" protein-protein interaction"> protein-protein interaction</a> </p> <a href="https://publications.waset.org/abstracts/81407/combining-in-vitro-protein-expression-with-alphalisa-technology-to-study-protein-protein-interaction" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/81407.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">236</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">3595</span> Modeling Generalization in the Acquired Equivalence Paradigm with the Successor Representation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Troy%20M.%20Houser">Troy M. Houser</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The successor representation balances flexible and efficient reinforcement learning by learning to predict the future, given the present. As such, the successor representation models stimuli as what future states they lead to. Therefore, two stimuli that are perceptually dissimilar but lead to the same future state will come to be represented more similarly. This is very similar to an older behavioral paradigm -the acquired equivalence paradigm, which measures the generalization of learned associations. Here, we test via computational modeling the plausibility that the successor representation is the mechanism by which people generalize knowledge learned in the acquired equivalence paradigm. Computational evidence suggests that this is a plausible mechanism for acquired equivalence and thus can guide future empirical work on individual differences in associative-based generalization. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=acquired%20equivalence" title="acquired equivalence">acquired equivalence</a>, <a href="https://publications.waset.org/abstracts/search?q=successor%20representation" title=" successor representation"> successor representation</a>, <a href="https://publications.waset.org/abstracts/search?q=generalization" title=" generalization"> generalization</a>, <a href="https://publications.waset.org/abstracts/search?q=decision-making" title=" decision-making"> decision-making</a> </p> <a href="https://publications.waset.org/abstracts/190117/modeling-generalization-in-the-acquired-equivalence-paradigm-with-the-successor-representation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/190117.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">27</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">3594</span> An Efficient Algorithm for Global Alignment of Protein-Protein Interaction Networks</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Duc%20Dong%20Do">Duc Dong Do</a>, <a href="https://publications.waset.org/abstracts/search?q=Ngoc%20Ha%20Tran"> Ngoc Ha Tran</a>, <a href="https://publications.waset.org/abstracts/search?q=Thanh%20Hai%20Dang"> Thanh Hai Dang</a>, <a href="https://publications.waset.org/abstracts/search?q=Cao%20Cuong%20Dang"> Cao Cuong Dang</a>, <a href="https://publications.waset.org/abstracts/search?q=Xuan%20Huan%20Hoang"> Xuan Huan Hoang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Global aligning two protein-protein interaction networks is an essentially important task in bioinformatics/computational biology field of study. It is a challenging and widely studied research topic in recent years. Accurately aligned networks allow us to identify functional modules of proteins and/ororthologous proteins from which unknown functions of a protein can be inferred. We here introduce a novel efficient heuristic global network alignment algorithm called FASTAn, including two phases: the first to construct an initial alignment and the second to improve such alignment by exerting a local optimization repeated procedure. The experimental results demonstrated that FASTAn outperformed the state-of-the-art global network alignment algorithm namely SPINAL in terms of both commonly used objective scores and the run-time. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=FASTAn" title="FASTAn">FASTAn</a>, <a href="https://publications.waset.org/abstracts/search?q=Heuristic%20algorithm" title=" Heuristic algorithm"> Heuristic algorithm</a>, <a href="https://publications.waset.org/abstracts/search?q=biological%20network%20alignment" title=" biological network alignment"> biological network alignment</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-protein%20interaction%20networks" title=" protein-protein interaction networks"> protein-protein interaction networks</a> </p> <a href="https://publications.waset.org/abstracts/17228/an-efficient-algorithm-for-global-alignment-of-protein-protein-interaction-networks" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/17228.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">603</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">3593</span> DNpro: A Deep Learning Network Approach to Predicting Protein Stability Changes Induced by Single-Site Mutations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Xiao%20Zhou">Xiao Zhou</a>, <a href="https://publications.waset.org/abstracts/search?q=Jianlin%20Cheng"> Jianlin Cheng</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A single amino acid mutation can have a significant impact on the stability of protein structure. Thus, the prediction of protein stability change induced by single site mutations is critical and useful for studying protein function and structure. Here, we presented a deep learning network with the dropout technique for predicting protein stability changes upon single amino acid substitution. While using only protein sequence as input, the overall prediction accuracy of the method on a standard benchmark is >85%, which is higher than existing sequence-based methods and is comparable to the methods that use not only protein sequence but also tertiary structure, pH value and temperature. The results demonstrate that deep learning is a promising technique for protein stability prediction. The good performance of this sequence-based method makes it a valuable tool for predicting the impact of mutations on most proteins whose experimental structures are not available. Both the downloadable software package and the user-friendly web server (DNpro) that implement the method for predicting protein stability changes induced by amino acid mutations are freely available for the community to use. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=bioinformatics" title="bioinformatics">bioinformatics</a>, <a href="https://publications.waset.org/abstracts/search?q=deep%20learning" title=" deep learning"> deep learning</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20stability%20prediction" title=" protein stability prediction"> protein stability prediction</a>, <a href="https://publications.waset.org/abstracts/search?q=biological%20data%20mining" title=" biological data mining"> biological data mining</a> </p> <a href="https://publications.waset.org/abstracts/48058/dnpro-a-deep-learning-network-approach-to-predicting-protein-stability-changes-induced-by-single-site-mutations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/48058.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">467</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">3592</span> A Dynamic Neural Network Model for Accurate Detection of Masked Faces</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Oladapo%20Tolulope%20Ibitoye">Oladapo Tolulope Ibitoye</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Neural networks have become prominent and widely engaged in algorithmic-based machine learning networks. They are perfect in solving day-to-day issues to a certain extent. Neural networks are computing systems with several interconnected nodes. One of the numerous areas of application of neural networks is object detection. This is a prominent area due to the coronavirus disease pandemic and the post-pandemic phases. Wearing a face mask in public slows the spread of the virus, according to experts’ submission. This calls for the development of a reliable and effective model for detecting face masks on people's faces during compliance checks. The existing neural network models for facemask detection are characterized by their black-box nature and large dataset requirement. The highlighted challenges have compromised the performance of the existing models. The proposed model utilized Faster R-CNN Model on Inception V3 backbone to reduce system complexity and dataset requirement. The model was trained and validated with very few datasets and evaluation results shows an overall accuracy of 96% regardless of skin tone. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=convolutional%20neural%20network" title="convolutional neural network">convolutional neural network</a>, <a href="https://publications.waset.org/abstracts/search?q=face%20detection" title=" face detection"> face detection</a>, <a href="https://publications.waset.org/abstracts/search?q=face%20mask" title=" face mask"> face mask</a>, <a href="https://publications.waset.org/abstracts/search?q=masked%20faces" title=" masked faces"> masked faces</a> </p> <a href="https://publications.waset.org/abstracts/163866/a-dynamic-neural-network-model-for-accurate-detection-of-masked-faces" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/163866.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">68</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">3591</span> Magnetic Nanoparticles for Protein C Purification</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Duygu%20%C3%87imen">Duygu Çimen</a>, <a href="https://publications.waset.org/abstracts/search?q=Nilay%20Bereli"> Nilay Bereli</a>, <a href="https://publications.waset.org/abstracts/search?q=Adil%20Denizli"> Adil Denizli</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this study is to synthesis magnetic nanoparticles for purify protein C. For this aim, N-Methacryloyl-(L)-histidine methyl ester (MAH) containing 2-hydroxyethyl methacrylate (HEMA) based magnetic nanoparticles were synthesized by using micro-emulsion polymerization technique for templating protein C via metal chelation. The obtained nanoparticles were characterized with Fourier transform infrared spectroscopy (FTIR), transmission electron microscopy (TEM), zeta-size analysis and electron spin resonance (ESR) spectroscopy. After that, they were used for protein C purification from aqueous solution to evaluate/optimize the adsorption condition. Hereby, the effecting factors such as concentration, pH, ionic strength, temperature, and reusability were evaluated. As the last step, protein C was determined with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=immobilized%20metal%20affinity%20chromatography%20%28IMAC%29" title="immobilized metal affinity chromatography (IMAC)">immobilized metal affinity chromatography (IMAC)</a>, <a href="https://publications.waset.org/abstracts/search?q=magnetic%20nanoparticle" title=" magnetic nanoparticle"> magnetic nanoparticle</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20C" title=" protein C"> protein C</a>, <a href="https://publications.waset.org/abstracts/search?q=hydroxyethyl%20methacrylate%20%28HEMA%29" title=" hydroxyethyl methacrylate (HEMA)"> hydroxyethyl methacrylate (HEMA)</a> </p> <a href="https://publications.waset.org/abstracts/30767/magnetic-nanoparticles-for-protein-c-purification" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/30767.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">424</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%20masked%20representation&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=5">5</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=6">6</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=7">7</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=8">8</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=9">9</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=10">10</a></li> <li class="page-item disabled"><span class="page-link">...</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=120">120</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=121">121</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation&page=2" rel="next">&rsaquo;</a></li> </ul> </div> </main> <footer> <div id="infolinks" class="pt-3 pb-2"> <div class="container"> <div style="background-color:#f5f5f5;" class="p-3"> <div class="row"> <div class="col-md-2"> <ul class="list-unstyled"> About <li><a href="https://waset.org/page/support">About Us</a></li> <li><a href="https://waset.org/page/support#legal-information">Legal</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/WASET-16th-foundational-anniversary.pdf">WASET celebrates its 16th foundational anniversary</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Account <li><a href="https://waset.org/profile">My Account</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Explore <li><a href="https://waset.org/disciplines">Disciplines</a></li> <li><a href="https://waset.org/conferences">Conferences</a></li> <li><a href="https://waset.org/conference-programs">Conference Program</a></li> <li><a href="https://waset.org/committees">Committees</a></li> <li><a href="https://publications.waset.org">Publications</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Research <li><a href="https://publications.waset.org/abstracts">Abstracts</a></li> <li><a href="https://publications.waset.org">Periodicals</a></li> <li><a href="https://publications.waset.org/archive">Archive</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Open Science <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Philosophy.pdf">Open Science Philosophy</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Award.pdf">Open Science Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Society-Open-Science-and-Open-Innovation.pdf">Open Innovation</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Postdoctoral-Fellowship-Award.pdf">Postdoctoral Fellowship Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Scholarly-Research-Review.pdf">Scholarly Research Review</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Support <li><a href="https://waset.org/page/support">Support</a></li> <li><a href="https://waset.org/profile/messages/create">Contact Us</a></li> <li><a href="https://waset.org/profile/messages/create">Report Abuse</a></li> </ul> </div> </div> </div> </div> </div> <div class="container text-center"> <hr style="margin-top:0;margin-bottom:.3rem;"> <a href="https://creativecommons.org/licenses/by/4.0/" target="_blank" class="text-muted small">Creative Commons Attribution 4.0 International License</a> <div id="copy" class="mt-2">© 2024 World Academy of Science, Engineering and Technology</div> </div> </footer> <a href="javascript:" id="return-to-top"><i class="fas fa-arrow-up"></i></a> <div class="modal" id="modal-template"> <div class="modal-dialog"> <div class="modal-content"> <div class="row m-0 mt-1"> <div class="col-md-12"> <button type="button" class="close" data-dismiss="modal" aria-label="Close"><span aria-hidden="true">×</span></button> </div> </div> <div class="modal-body"></div> </div> </div> </div> <script src="https://cdn.waset.org/static/plugins/jquery-3.3.1.min.js"></script> <script src="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/js/bootstrap.bundle.min.js"></script> <script src="https://cdn.waset.org/static/js/site.js?v=150220211556"></script> <script> jQuery(document).ready(function() { /*jQuery.get("https://publications.waset.org/xhr/user-menu", function (response) { jQuery('#mainNavMenu').append(response); });*/ jQuery.get({ url: "https://publications.waset.org/xhr/user-menu", cache: false }).then(function(response){ jQuery('#mainNavMenu').append(response); }); }); </script> </body> </html>