Scientific Program | Genetic and Protein Engineering 2016 | Biochemistry Conferences | USA | Worldwide Events | Europe | Canada | UK

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Program</h2> <div class="well well-sm content-box-dotted clearfix"> <div class="col-md-8 col-sm-6"> <p>Conference Series Ltd invites all the participants across the globe to attend 2<sup>nd</sup> International Conference on Genetic and Protein Engineering Atlanta, Georgia, USA.</p> </div> <div class="col-md-4 col-sm-6 help-desk"><a class="btn btn-danger" href="https://protein-engineering.conferenceseries.com/abstract-submission.php" title="Click for more information">Submit your Abstract</a> <h5>or e-mail to <i class="fa fa-arrow-down"></i></h5> <p> <i class="fa fa-envelope-o"></i> <a href="mailto:events@conferenceseries.com">events@conferenceseries.com</a><br> <i class="fa fa-envelope-o"></i> <a href="mailto:proteinengineering@biochemistryconferences.com">proteinengineering@biochemistryconferences.com</a><br> <i class="fa fa-envelope-o"></i> <a href="mailto:proteinengineering@insightconferences.com">proteinengineering@insightconferences.com</a><br> </div> </div> <div class="show-special day-schedule text-center clearfix"> <div class="col-md-4 col-sm-4"> <a class="btn btn-success" href="https://protein-engineering.conferenceseries.com/2016/scientific-program.php?day=1&sid=2713&date=2016-11-14" title="Click for more information">Scientific Program <span class="badge">Day 1</span></a> </div> <div class="col-md-4 col-sm-4"> <a class="btn btn-success" href="https://protein-engineering.conferenceseries.com/2016/scientific-program.php?day=2&sid=2717&date=2016-11-15" title="Click for more information">Scientific Program <span class="badge">Day 2</span></a> </div> </div> <article class="scientific-prog"> <h3 class="heading heading-out">Day 2 : <time datetime="2015-12-07">November 15, 2016</time><span class="heading-shadow"></span></h3> <section class="col-md-12 content-box-dotted"> <div class="affiliation bs-callout"> <h4>Keynote Forum</h4> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/abdellah-salhi-university-of-essex-uk" >Abdellah Salhi</a></h4> <p>University of Essex, Uk</p> <h6>Keynote: <a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/abstract/2016/a-deterministic-algorithm-for-protein-sequence-detection" >A deterministic algorithm for protein sequence detection</a></h6> <p>Time : <b> 10:00-10:30</b></p> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Abdellah-Salhi-3604.jpg" alt="Conference Series Protein Engineering 2016 International Conference Keynote Speaker Abdellah Salhi photo" title="Abdellah Salhi" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><p style="text-align: justify;"> Abdellah Salhi is Professor of Operational Research. He was educated to degree level at the University of Constantine, Algeria. He obtained his PhD on Interior-Point Methods from the University of Aston in Birmingham, UK.  His research interests are in the design, analysis, implementation and application of OR algorithms. Application areas include scheduling, decision making, data-mining and bioinformatics. He has led a number of research projects and contributes to the ESRC funded Business and Local Government Data Research Centre. He has published over 80 papers. He is currently the Head of the Department of Mathematical Science of Essex University, UK.</p> </p> <h5>Abstract:</h5> <p><p style="text-align: justify;"> <a href="https://protein-engineering.conferenceseries.com">Sequence analysis</a> is at the core of <a href="https://protein-engineering.conferenceseries.com">bioinformatics.</a> Many algorithms have been developed for the purpose, which, almost invariably, try to measure the similarity between sequences of symbols drawn from finite sets but with varied cardinalities. These algorithms are in two broad classes: deterministic and stochastic. Deterministic algorithms are often hard to implement and are slow in practice. <a href="https://protein-engineering.conferenceseries.com">Stochastic algorithms</a>, on the other hand, are relatively easier to implement and are efficient. However, they do not guarantee to find the correct solution when it exists. This limits their use particularly where it is essential to know the exact solution as in medical situations. The inherent uncertainty in the outcomes of deterministic approaches is exacerbated by the need to arbitrarily set a number of parameters on which they depend. Default values of these parameters are often inappropriate outside the context in which they were estimated. There is, therefore, room for deterministic algorithms particularly when the time constraint is soft. In this paper we highlight the limitations of stochastics algorithms on probably the most prominent genomics search tool, namely the Basic Local Search Tool or <a href="https://protein-engineering.conferenceseries.com">BLAST</a>. We then present an algorithm which, besides being deterministic, is easy to understand and implement. We illustrate it on <a href="https://protein-engineering.conferenceseries.com">Shotgun Proteomics Data </a>and compare it with a number of other well-known sequence comparison algorithms such as the Needleman-Wunch and Smith-Waterman algorithms.</p> </p> </div> </div> </div> </section> <section class="col-md-12 content-box-dotted"> <div class="affiliation bs-callout"> <h4>Keynote Forum</h4> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/frederic-cadet-peaccel-france" >Frederic CADET </a></h4> <p>Peaccel, France</p> <h6>Keynote: <a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/abstract/2016/disruptive-mixed-in-vitro-in-silico-approach-for-protein-engineering-and-screening" >Disruptive mixed in vitro-in silico approach for protein engineering and screening</a></h6> <p>Time : <b>10:30-11:00</b></p> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Frederic-CADET--3605.jpg" alt="Conference Series Protein Engineering 2016 International Conference Keynote Speaker Frederic CADET photo" title="Frederic CADET " class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><p style="text-align: justify;"> Prof Dr Frédéric CADET (PEACCEL, Paris, France): Vice President Research & Development of the company Peaccel (Protein Engineering ACCELerator: <a href="http://www.peaccel.com/">http://www.peaccel.com</a>). Ph.D (specialization in: Protein Engineering, Data mining, Biosimulation). From 2004 to 2008, as an “<em>Executive School, University & Research Commissioner</em>”, he managed a budget of 1.3 billion Euros and was responsible for 32,000 employees. Former Chairman of the ERA Nets (European Research Area Networks) <em>NetBIOME</em>. He has developed pioneering research activities in bioinformatics. Author of over 70 publications and referee for 17 international scientific journals. Organizing Committee Member for « <em>2nd International Conference on "Genetic and Protein Engineering</em>”, November 14-16, 2016 Atlanta, USA. </p> </p> <h5>Abstract:</h5> <p><p style="text-align: justify;"> We present a strategy that combines <a href="https://protein-engineering.conferenceseries.com">wet-lab</a> experimentation and computational <a href="https://protein-engineering.conferenceseries.com">protein design</a> for engineering polypeptide chains. The protein sequences were numerically coded and then processed using <a href="https://protein-engineering.conferenceseries.com">Fourier Transform</a> (FT). Fourier coefficients were used to calculate the energy spectra called "<a href="https://protein-engineering.conferenceseries.com">protein spectrum</a>". We use the protein spectrum to model the biological activity/fitness of <a href="https://protein-engineering.conferenceseries.com">protein</a> from sequence data. We assume that the protein fitness (catalytic efficacy, thermostabilty, binding affinity, aggregation, stability…) is not purely local, but globally distributed over the linear sequence of the protein. Our patented method does not require any protein 3D structure information and find patterns that correlate with changes in <a href="https://protein-engineering.conferenceseries.com">protein activity</a> (or fitness) upon amino acids residue substitutions. A minimal wet lab data sampled from mutation libraries (single or multiple points mutations) were used as learning data sets in heuristic approaches that were applied to build predictive models. We show the performance of the approach on designed libraries for 3 examples: enantioselectivity, thermostability and binding affinity. We can screen up to 1 billion protein variants (10^9).</p> </p> </div> </div> </div> </section> <div class="well well-sm col-md-12 content-box-dotted"> <div class="content-box tracks" style="clear:both"> <ul class="list-group show"> <li class="list-group-item">Track 4: Enzyme Engineering | Track 5: Recombinant Protein Expression</li> </ul> <h5>Location: Chittahoochee B</h5> </div> <section> <div class="col-md-12" > <div class="affiliation bs-callout speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/7309-Session-Photo-T.jpg" alt="Speaker" title="Frederic CADET" class="img-responsive thumbnail pull-left"> <div class="bio"> <h4>Chair</h4> <h4>Frederic CADET</h4> <p>PEACCEL-Protein Engineering Accelerator, France</p> </div> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4>Session Introduction</h4> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/d-l-savithramma-university-of-agricultural-sciences-india-2081783623" >D.L. Savithramma</a></h4> <p>University of Agricultural Sciences, India</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/development-and-characterization-of-newly-developed-genomic-ssr-markers-in-mungbean-vignaradiata-l-wilczek" >Development and characterization of newly developed genomic SSR markers in mungbean (Vignaradiata(L.) Wilczek)</a> </h6> <p>Time : <b>11:20-11:50</b></p> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-DL-Savithramma-47533.jpg" alt="Speaker" title="D.L. Savithramma" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><p style="text-align: justify;"> D.L.Savithramma has completed her PhD at the age of 35 years from University of Agricultural Sciences, Bangalore, India and postdoctoral studies as a Biotechnology National Associate from Indian Institute Science, Bangalore, India. She is a Professor of Genetics and Plant Breeding at University of Agricultural Sciences, Bangalore, India, one of the premier Agricultural University in India. She has published more than 70 papers in reputed journals and has released seven varieties in Vegetable cowpea, seed cowpea, Peanut and Chrysanthemum</p> </p> <h5>Abstract:</h5> <p><p style="text-align: justify;"> <a href="https://protein-engineering.conferenceseries.com"> Simple sequence repeat</a> (SSR) markers are a major molecular tool for genetic and genomic research that have been extensively developed and used in major crops. However, few are available in mungbean (<em>Vigna radiata</em>(L.) Wilczek), an economically important <a href="https://protein-engineering.conferenceseries.com">protein</a> rich(22-24%) edible food <a href="https://protein-engineering.conferenceseries.com">legume</a> of South and Southeast Asia. Mung bean is a self-pollinating diploid grain legume with the genome size of 560 Mb. Therefore, the application of molecular markers can play key role in direct improvement of mung bean. Development and use of molecular markers in the species are limited. The major objective of this study was development for a set of simple sequence repeat (SSR) markers based on construction of SSR-enriched genomic DNA libraries, sequencing, and validation of designed primers. Mungbean genotypes Chinamung and BL 849 were used to isolate <a href="https://protein-engineering.conferenceseries.com">DNA</a> for constructing SSR-enriched genomic libraries. More than 200 positive clones were purified and they were sequenced using vector specific primer.Quality of all DNA sequences was analyzed. After trimming off the vector sequences, all the sequences were placed in a fasta file for further analysis with the CAP3 program to categorize the sequences into contiguous sequences (contigs) and singletons(non repeating). The two categories of sequences were run separately with the SSR Locator program for SSR detection and primer designing. The parameters for the primer design were given as  amplicon size in 140–350 bp, primer length of 18–22 bases with 20 as the optimum, annealing temperature of 55–61°C with an optimum of 59°C, GC clamp 0, G/C content 45–50 %, start and end point automatic scan and end stability at 250. A total of 40 primer pairs were designed from the microsatellite-containing sequences. Newly synthesized 40 mung bean SSR primers were used for genetic diversity studies with 24 genotypes and dendrogram was constructed. Out of 40 designed <a href="https://protein-engineering.conferenceseries.com">prime</a>r pairs 26 primer pairs were found to amplify bands of the expected sizes while eleven primers failed to amplify and three primers produced monomorphic bands. The overall size of the amplified product varied from 110 to 400 bp. The coefficient of genetic dissimilarity ranged from 0.159 to 0.536. Pairwise estimates of dissimilarity ranged from 0.14 to 0.90 and the average dissimilarity among all 24 genotypes was 0.365. Two genotypes LM 192 and IC325738 were the closest related genotypes with the lowest dissimilarity index of 0.159. The highest dissimilarity (0.536) was observed between genotypes WBM and SML 348. The SSR markers developed in the study are highly valuable for molecular and traditional breeding research.</p> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/du-qing-fresh-skyright-international-science-and-technology-co-ltd-china" >Du Qing</a></h4> <p>Fresh-skyright International Science and Technology Co. Ltd., China</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/the-preparation-and-application-of-charming-ubiquinone" >The preparation and application of charming ubiquinone</a> </h6> <p>Time : <b>11:50-12:20</b></p> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Du-Qing-48717.jpg" alt="Speaker" title="Du Qing" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><div> Duqing has completed her PhD in the year 2015 in the Major of pharmacognosy from the Institute of Medicinal Plant Development, Chinese Academy of Medical Sciences and Peking Union Medical College. She also did Post-doctoral studies at the Institute of Genetics and Developmental Biology, Beijing, China until the April of 2016. She is the Member of American Society of Plant Biologists and Chinese Society for Cell Biology. She is a Pharmacist and the Member of Chinese Pharmacist Association. She has published more than 5 papers in the BMC and Chinese famous journals in research groups</div> </p> <h5>Abstract:</h5> <p><div style="text-align: justify;"> <a href="https://protein-engineering.conferenceseries.com">Ubiquinone</a> (coenzyme Q) is the kinds of compound which are classified into the type of <a href="https://protein-engineering.conferenceseries.com">lipid</a> soluble quinone from the structure. Th ey have different structures because of the number of isoprenes present. We can know some research information about CoQ0, CoQ1, CoQ2, CoQ6, CoQ7, CoQ8, CoQ9, CoQ10 which has been synthesized or extracted from the plants by the way of chemical synthesis. However, the method of chemosynthesis has the limited efficiency and higher cost during the course of procedure; in addition, for the extraction from the <a href="https://protein-engineering.conferenceseries.com">natural medicine</a>, the same problem exists. Therefore,with the development of genomics and microbiome technology, more and more chemistry can be induced and extracted from the diverse biological creature or <a href="https://protein-engineering.conferenceseries.com">microzyme</a> for the intrinsic mechanism which is found by the international scientists.Coenzyme Q exists in three redox forms, fully oxidized (ubiquinone), semiquinone radical (ubisemiquinone) and fully reduced (ubiquinol). In addition, coenzyme Q can form micellar aggregates while working with together in cell-free system; however, in the living cell, coenzyme can dissolve in lipid bilayers and bound to proteins. Coenzyme Q is the center and an essential component of the mitochondrial electron transport chain. Coenzyme Q can closely combine with the protein in the respiratory chain to have the action from the intrinsic mechanism. So from the in vivo and in vitro studies, coenzyme Q has important applications in the study of pharmacology & clinics; such as, treating cardiovascular diseases, Parkinson’s disease and Huntington’s disease, etc. I would like to give the presentation in the review of the preparation and application of <a href="https://protein-engineering.conferenceseries.com">coenzyme Q</a> in order to be supported by the experts and professors who are always interested in the study on the relative area and give us better opinions or investment on the research projects.</div> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/d-l-savithramma-university-of-agricultural-sciences-india-705190119" >D.L. Savithramma </a></h4> <p>University of Agricultural Sciences, India</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/single-marker-analysis-in-mungbean-vigna-radiata-l-wilczek-for-powdery-mildew-disease-resistance-and-yield-attributing-traits" >Single marker analysis in mungbean(Vigna radiata (L.) Wilczek) for powdery mildew disease resistance and yield attributing traits</a> </h6> <p>Time : <b>12:20:12:50</b></p> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-DL-Savithramma--47536.jpg" alt="Speaker" title="D.L. Savithramma " class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><p style="text-align: justify;"> D.L.Savithramma has completed her PhD at the age of 35 years from University of Agricultural Sciences, Bangalore, India and postdoctoral studies as a Biotechnology National Associate from Indian Institute Science, Bangalore, India. She is a Professor of Genetics and Plant Breeding at University of Agricultural Sciences, Bangalore, India,  one of the premier Agricultural University in India. She has published more than 70 papers in reputed journals and has released seven varieties in Vegetable cowpea, seed cowpea, Peanut and Chrysanthemum</p> </p> <h5>Abstract:</h5> <p><p style="text-align: justify;"> Pulse crops have been shown to be an excellent source of <a href="https://protein-engineering.conferenceseries.com">dietary</a><a href="https://protein-engineering.conferenceseries.com"> protein </a>important for the human diet and play a key role in crop rotation due to their ability to fix nitrogen. Since all recommended greengram varieties are susceptible to the disease, <a href="https://protein-engineering.conferenceseries.com">plant breeders</a> are interested in developing resistant varieties through both conventional and marker-assisted breeding. The genetic nature of a trait, phenotypic data and genotypic data from molecular markers was studied by detecting associations between markers and traits and determined the number and nature of a gene/quantitative trait locus (QTL) controlling a trait. Mung bean germplasm screening was done for powdery mildew disease resistance and yield related traits and genotypes were selected. Hybridization was done between powdery mildew resistant BL 849 (male parent) and Chinamung (female parent) which issusceptible but high yielding. The F<sub>1 </sub>generation was developed and forwarded to F<sub>2</sub>. Individuals of F<sub>2</sub>generation of this cross were screened for powdery mildew disease. The F<sub>2</sub> individuals were also classified into three marker classes. The mean disease score of the 94 F<sub>2 </sub>individuals belonging to each of the marker classes were computed. The significance of differences among the three marker classes for disease score and productivity traits were tested using F test through <a href="https://protein-engineering.conferenceseries.com">ANOVA approach</a>. The relationship between molecular markers and phenotypic scores were analysed by single marker analysis to identify SSR markers that had significant association with powdery mildew disease reaction severity scoresin greengram.For the markers DMBSSR 130 and VM 27, chi square (χ2) was non significant suggesting that the distribution of the genotypic data fit Mendel’s segregation ratio of 1:2:1. Single marker analysis for <a href="https://protein-engineering.conferenceseries.com">SSR marker</a> DMBSSR 130 and VM 27 showed very high association among the marker classes and the powdery mildew resistant type in F<sub>2</sub> mapping population.  In the single marker analysis, the markers GBSSRMB 14 and DMBSSR 34 were found to be highly linkedwithtraits<em>viz</em>., number of pods per plant, pod yield per plant and seed yield per plant in F<sub>2</sub> segregating population. This indicates that the same gene is controlling the expression of these characters. Moreover, phenotypically these characters have more association with each other. Hence these markers may be useful for marker assisted breeding programme. GBSSRMB 14 was also linked with number of pods per plant and number of clusters per plant. MBSSR 42 was associated with seed yield, pod yield and number of clusters per plant. The marker GBSSR MB 87 was found to be associated with number of branches per plant.  Molecular markers linked with QTL/major genes for traits of interest are being routinely developed in several crops. However, non-availability of mapping populations and substantial time needed to develop such populations are sometimes major limitations in the identification of <a href="https://protein-engineering.conferenceseries.com">molecular markers </a>for specific traits. Another limitation is the absence of tight linkage between marker and traits observed in these studies. Also, it is difficult to eliminate false positives with available methods. Therefore, markers identified during the present study need to be subjected to validation and/or functional analysis of respective traits.</p> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/krishnamurthy-n-university-of-agricultural-sciences-india" >Krishnamurthy N</a></h4> <p>University of Agricultural Sciences, India</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/genotypic-evaluation-of-guar-cyamopsis-tetragonoloba-l-for-protein-gum-and-seed-yield-traits" >Genotypic evaluation of guar (Cyamopsis tetragonoloba l.) for protein, gum and seed yield traits</a> </h6> <p>Time : <b>14:00-14:30</b></p> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Krishnamurthy-N-48718.jpg" alt="Speaker" title="Krishnamurthy N" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><div style="text-align: justify;"> KRISHNAMURTHY, N., Presently Serving as Dean (Post Graduate Studies), University of Agricultural Sciences, Bangalore. Served the University for 38 years in various capacities as Researcher, Extension Specialist, Chief Agronomist, Professor(Head), University Head (Discipline of Agronomy). Published more than 60 research papers, 3 books and prepared many UG Laboratory manuals. Guided 14 M.Sc.(Agri.) & 9 Ph.D students as Chairman, member for 37 M.Sc.(Agri.) & 19 Ph.D students. Academic referee for many standard scientific journals. Visited many countries; Indonesia, The Netherlands, Turkey, Malaysia, London, France, Brussel, Belgium, Hamberg, Germany and Presented scientific research papers in the International conferences. He served as Chairman (Technical Committee), Biodiversity Board, Chairman (Knowledge Enhancement Committee), Institute of Agricultural Technologies, Vice-President & Secretary (Alumni Association) and as member in many selection committee of Government and public undertakings for various technical posts and also life member for many scientific journals</div> </p> <h5>Abstract:</h5> <p><div style="text-align: justify;"> Guar (Cyamopsis tetragonoloba L.) being an important legume is mainly utilized as vegetable crop. Currently, it is gaining importance in industry as guar gum due to higher <a href="https://protein-engineering.conferenceseries.com">galactomannan</a> content in the seed endosperm. Apart, the crop is rich in protein content (24-28%) and thus it can be used as a good <a href="https://protein-engineering.conferenceseries.com">protein</a> source. Developing good genotypes for the vagarious climatic condition is important. In view of this, to provide raw materials for the industries, an experiment was conducted during 2013 and 2014 at GKVK, Bengaluru, India to evaluate good guar genotypes for protein, gum and seed yield traits. The experiment was laid out in split-split plot design consisting of three dates of sowing in main plots (July fi rst fortnight, July second fortnight and August first fortnight), 2 spacings (30 cm x 15 cm and 45 cm x 15 cm) in sub-plots and 4 genotypes (HG- 563, HG-365, RGC-1006 and Tulsi) in sub-sub plots and was replicated thrice. Results indicated that among the genotypes, the genotype HG-563 recorded significantly higher <a href="https://protein-engineering.conferenceseries.com">protein content</a> of 26.35% over other <a href="https://protein-engineering.conferenceseries.com">genotypes</a> and lower protein content of 24.51% was recorded with Tulsi genotype. The same genotypes also recorded higher and lower protein yield of 178.1 and 112.5 kgha-1, respectively. Similarly, the genotype HG-563 recorded significantly higher <a href="https://protein-engineering.conferenceseries.com">gum content</a> and yield of 30.28% and 204.7 kgha-1, respectively. Th e higher protein and gum yield was mainly attributed to better growth components, which helped in better translocation of photosynthates from source to sink lead to higher protein in seeds. Significantly higher seed yield of</div> <div style="text-align: justify;"> guar was registered with HG-563 (676 kgha-1) as compared to Tulsi genotype</div> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/madhu-s-v-university-of-agricultural-sciences-india" >Madhu S V</a></h4> <p>University of Agricultural Sciences, India</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/identifi-cation-of-drought-tolerant-groundnut-arachis-hypogaea-genotypes-under-stress-and-control-conditions-through-gravimetric-studies" >Identifi cation of drought tolerant groundnut (Arachis hypogaea) genotypes under stress and control conditions through gravimetric studies</a> </h6> <p>Time : <b>14:30-15:00</b></p> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Madhu-S-V-48719.jpg" alt="Speaker" title="Madhu S V" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p></p> <h5>Abstract:</h5> <p><div style="text-align: justify;"> Plant root is one of the major organs for water and nutrient uptake from soil. Root development and amount of water absorption from the soil are closely related. Under drought condition, the success of crop plants oft en depends on growth of roots. In the present study, gravimetric experiment was conducted to evaluate the yield potential of released and pre-released groundnut genotypes. Root growth parameters such as root length, shoot length, shoot weight, leaf length, root volume and dry root weight were recorded in fi ve genotypes viz., KCG-2, TMV-2, GKVK-5, GKVK-3 and GKVK-13 under controlled and water stress conditions in pot experiment at University of Agricultural Sciences, Bangalore, India. Stress was imposed for</div> <div style="text-align: justify;"> 20 days during fl owering stage by balancing the amount of water applied to make it 50% stress. Analysis of variance revealed highly signifi cant diff erences for the traits observed indicating the existence of variability in the material selected. In controlled condition all the root traits exhibited higher mean values over stress condition in the genotypes studied except in GKVK-5</div> <div style="text-align: justify;"> for root dry weight. In stress treatment GKVK-5, GKVK-3 and GKVK-13 genotypes exhibited higher mean values for root volume, root dry weight and root length. Genotypes GKVK-5, TMV-2 and KCG-2 recorded higher mean for shoot weight and leaf length. Among all genotypes GKVK-5 was identifi ed as high yielding with 2.8 to 3.0 t/ ha, with low to moderate Δ13C (17.53) and high δ18O (31.24) and low specifi c leaf area (107.76 cm2/g) and was found to have higher water use effi ciency or to be drought tolerant genotype indicating effective partitioning of the accumulated biomass towards root and shoot, while diverting relatively lesser towards shoot biomass. Hence, breeding for root development proved to be eff ective in increasing crop water use effi ciency and drought tolerance.</div> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/n-marappa-college-of-sericulture-india" >N. Marappa </a></h4> <p>College of Sericulture, India</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/screening-of-elite-cowpea-genotypes-for-zinc-iron-protein-and-yield-attributes" >Screening of elite cowpea genotypes for zinc, iron, protein and yield attributes</a> </h6> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-N-Marappa--47531.jpeg" alt="Speaker" title="N. Marappa " class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p></p> <h5>Abstract:</h5> <p><p style="text-align: justify;"> Cowpea (<em>Vigna unguiculata</em>) with chromosome number 2n=22 is a multipurpose grain legume crop grown throughout sub-tropical areas of the world. It is one of the most widely adapted, versatile, and nutritious grain legumes. It’s a good source of protein, carbohydrate, fat, vitamins and phosphorous. Cowpea is a cheapest source of vegetarian protein, development of high yielding cowpea varieties with high zinc, iron and protein will help fighting against malnutrition. Introduction of biofortified agricultural products and crop varieties with superior nutritional value are a prime low-cost crop improvement strategy for increasing the food sustainability. Though several options are available for augmenting mineral deficiencies of the soil, development of nutrient efficient genotypes seems be eco-friendly and long sustaining option to fight malnutrition. Keeping these aspects in mind, present investigation was carried at Department of Genetics and Plant Breeding, University of Agricultural Sciences, Bengaluru. Two hundred cowpea genotypes obtained from different sources were field screened for their phenotypic performance and also screened for zinc, iron, protein. Iron and Zinc contents in seeds of elite cowpea genotypes were analyzed using Atomic absorption spectrophotometry (AAS). The seed protein content was estimated using Kjeldahl method described in AOAC (1984).</p> <p style="text-align: justify;"> The analysis of variance (ANOVA) indicated significant difference for all the characters under consideration justifying the selection of genotypes for the study. Genetic variability estimates, Phenotypic co-efficient of variation (PCV) and Genotypic co-efficient of variation (GCV) were high for plant height, clusters per plant, pods per plant, pod yield per plant and seed yield per plant indicating the predominance of additive gene action and these traits offer scope for direct selection.</p> <p style="text-align: justify;">                 Highheritability estimates coupled with high genetic advance as <em>per cent</em> of meanwas observed for days to first flowering, days to fifty <em>per cent</em> flowering, plant height, primary branches per plant, clusters per plant, pods per plant, pod length, pod yield per plant, 100-seed weight and seed yield per plant suggesting that these characters are under the control of additive genes and phenotypic selection for these characters may be effective.Twenty-two lines were found to be rich zinc, iron and protein. Considering yield also, eighteen genotypes were found to be most promising. Themicronutrient range was found to be 15.8-48.6ppm, 49.6-150.2ppm and 22.03ppm to 26.21 %for zinc, iron and protein respectively. Genotype, PGCP-6 scored high zinc content of 48.6ppm, high iron of 137.2 ppm and 23.85% protein. Genotype KBC-6 was found to be rich in zinc 41.8ppm, iron 150.2ppm and 23.11 % protein. Local check KM5 scored zinc of 15.8ppm, iron 83.6ppm and protein 24.5%. The genotypes which showed high zinc were also associated with stay green colour even after maturity thus serving as phenotypic markers. Biochemical components associated with this trait needs to be identified which serve as marker to tag genotypes as zinc efficient. Molecular markers associated with stay green phenotype with high zinc needs to be identified. The two genotypes viz., PGCP-6 and KBC-6 were found to be most promising in terms of yield also thus could be used for further confirmation of their results and then used in crop improvement programmes.</p> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/ikram-ul-haq-gc-university-pakistan-2018315963" >Ikram ul Haq</a></h4> <p>GC University, Pakistan</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/cenc-a-multidomain-thermostable-gh9-processive-endoglucanase-from-clostridium-thermocellum-cloning-characterization-and-saccharification-studies-187" >CenC, a multidomain thermostable GH9 processive endoglucanase from clostridium thermocellum: cloning, characterization and saccharification studies</a> </h6> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Ikram-ul-Haq-47534.jpg" alt="Speaker" title="Ikram ul Haq" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><p style="text-align: justify;"> Prof. Dr. Ikram-ul-Haq (SI) has completed his Postdoc from Cornell University, New York, USA, and Ph.D. in Industrial Microbiology from University of the Punjab, Lahore, Pakistan. He has been the Dean, Faculty of Science and Technology and founding Director of Institute of Industrial Biotechnology, Government College University (GCU), Lahore. He has successfully completed 16Projects sponsored by Pakistan Science Foundation, Pakistan Atomic Energy Commission, HEC, GCU & Ministry of Science and Technology while 4 Projects are in process sponsored by MoST, PSF and Pakistan Academy of Sciences. He has published more than 309 papers in journals of international repute, with 1730 citations and has been serving as an editorial board member of reputed Journals </p> </p> <h5>Abstract:</h5> <p><p style="text-align: justify;"> The growing demands of bioenergy has led to the emphasis on novel cellulases to improve efficiency of biodegradation process of plant biomass. Therefore, a thermostable cellulolytic gene (CenC) with 3,675 bp was cloned from <em>Clostridium thermocellum </em>and over-expressed in <em>Escherichia coli</em> strain BL21 CodonPlus. It was attested that CenC belongs to glycoside hydrolase family 9 (GH9) with four binding domains, a processive endoglucanase. CenC was purified to homogeneity, producing a single band on SDS-PAGE corresponding to 137.11 kDa, by purification steps of heat treatment combined with ion-exchange chromatography. Purified enzyme displayed optimal activity at pH 6.0 and 70°C. CenC had a half-life of 24 min at 74°C, was stable upto 2 h at 60°C and over a pH range of 5.5-7.5. Enzyme showed high affinity towards various substrates and processively released cellobiose from cellulosic substrates confirmed by using HPLC technique. It efficiently hydrolyzed carboxymethyl cellulose (30 U/mg), β-glucan Barley (94 U/mg); also showed activity towards p-nitrophenyl-β-D-cellobioside (18 U/mg), birchwood xylan (19 U/mg), beechwood xylan (17.5 U/mg), avicel (9 U/mg), whatman filter paper (11 U/mg) and laminarin (3.3 U/mg). CenC exhibited K<sub>m</sub>, V<sub>max</sub>, K<sub>cat</sub>, V<sub>max </sub>K<sub>m</sub><sup>-1</sup> and K<sub>cat </sub>K<sub>m</sub><sup>-1 </sup>of 7.14 mM, 52.4 µmol mg<sup>-1</sup>min<sup>-1</sup>, 632.85 s<sup>-1</sup>, 7.34 min<sup>-1 </sup>and 88.63, respectively used CMC as substrate.Recombinant CenC saccharified pretreated wheat straw and bagasse to 5.12% and 7.31%, respectively at pH 7.0 and 45°C after 2 h incubation. Its thermostability, high catalytic efficiency and independence of inhibitors make CenC enzyme an appropriate candidate for industrial applications and cost-effective saccharification process</p> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/fatima-akram-gc-university-pakistan" >Fatima Akram</a></h4> <p>GC University, Pakistan</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/cloning-with-kinetic-and-thermodynamic-insight-of-a-novel-hyperthermostable---glucosidase-from-thermotoga-naphthophila-rku-10t-with-excellent-glucose-tolerance" >Cloning with kinetic and thermodynamic insight of a novel hyperthermostable Î²-glucosidase from thermotoga naphthophila RKU-10T with excellent glucose tolerance</a> </h6> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Fatima-Akram-47535.jpeg" alt="Speaker" title="Fatima Akram" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p></p> <h5>Abstract:</h5> <p><p style="text-align: justify;"> With a paradigm shift in industry, moving from natural fuels to alternative renewable resource utilization, the need of efficient thermostable cellulases are expected to increase in future. β-glucosidase, an essential member of cellulases that plays a critical role in cellulosic biomass degradation and in many biological processes. Therefore, a novel β-glucosidase gene encodes a protein (<em>Bgl</em>A) of 446 amino acid, belonging to glycoside hydrolase family 1 (GH1), was cloned from a hyperthermophilic bacterium <em>Thermotoga naphthophila</em> RKU-10<sup>T</sup> and over-expressed in <em>Escherichia coli</em> BL21 CodonPlus. An extracellular <em>Bgl</em>A with a molecular weight of 51.50 kDa, was purified to homogeneityby ion-exchange and hydrophobic interaction chromatography after heat treatment. Purified enzyme displayed optimal activity at pH 7.0 and 95°C. It was quite stable over a broad range of pH (6.0-9.0) and temperature (60-90°C), fairly stable up to 8 h at 80°C. Enzyme activity was stimulated by glucose concentration up to 600 mM and exhibited high glucose tolerance with a <em>K<sub>i</sub></em> value of 1200 mM.<em>Bgl</em>A showed great affinity towards<em>p</em>-nitrophenyl substrates and cellobiose. The <em>K</em><sub>m</sub>, <em>V</em><sub>max</sub> and <em>K</em><sub>cat</sub>values, against <em>p</em>NPG as substrate, were 1.5 mM, 297 mmol mg<sup>-1</sup>min<sup>-1</sup> and 1527778 s<sup>-1</sup>, respectively.Thermodynamic parameters for <em>p</em>NPG hydrolysis by <em>Bgl</em>A like âˆ†<em>H</em>*, âˆ†<em>G</em>* and âˆ†<em>S</em>* were calculated at 95°C as 25.7 kJ mol<sup>-1</sup>, 47.24 kJ mol<sup>-1</sup> and -58.6 J mol<sup>-1</sup> K<sup>-1</sup>, respectively. It displayed a half-life (t<sub>1/2</sub>) of 5.21 min at 97°C with denaturation parameters of enzyme including Δ<em>H*</em><sub>D</sub>, Δ<em>G</em>*<sub>D</sub> and Δ<em>S*</em><sub>D </sub>were 662.04 kJ mol<sup>-1</sup>, 110.10 kJ mol<sup>-1</sup>and 1.491 kJ mol<sup>-1 </sup>K<sup>-1</sup>, respectively. This is the first ever report on a highly glucose and thermotolerant β-glucosidase from<em>Thermotoga naphthophila</em>with high catalytic efficiency and low product inhibition, also exhibited independence of detergents and metal cations. All these significant features make <em>Bgl</em>A an appropriate candidate for biotechnological and industrial applications</p> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/kapil-vashisht-national-institute-of-malaria-research-icmr-new-delhi" >Kapil Vashisht</a></h4> <p>National Institute of Malaria Research, ICMR, New Delhi</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/engineering-nucleotide-specificity-of-succinyl-coa-synthetase-scs-in-blastocystis-the-emerging-role-of-gatekeeper-residues" >Engineering nucleotide specificity of succinyl-CoA Synthetase (SCS) in blastocystis: the emerging role of gatekeeper residues</a> </h6> <p>Time : <b>15:20-15:50</b></p> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Kapil-Vashisht-47532.jpg" alt="Speaker" title="Kapil Vashisht" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><p style="text-align: justify;"> Kapil Vashisht is a Senior Research Fellow at National Institute of Malaria Research, New Delhi, India and registered for Ph.D programe at Goa University, Goa, India. He is working under the supervision of Dr. Kailash C. Pandey, Scientist ‘E’, currently at National Institute for Research in Environmental Health, Bhopal, India. Recently he has submitted this interesting research in <em>Biochemistry</em> (Revised) as a first author and this study has also been filed for PCT at Indian Council of Medical Research, India (PCT/IN2015/000451). He is currently working to prove this concept in SCS of <em>P.falciparum</em> (another human parasite</p> </p> <h5>Abstract:</h5> <p><p style="text-align: justify;"> <a href="https://protein-engineering.conferenceseries.com">SCS</a> was discovered in 1958, there are extensive studies and crystal structures available, but mechanism of nucleotide specificity is still not clear. Hallmark concepts like “<a href="https://protein-engineering.conferenceseries.com">Lock and key</a>” and “<a href="https://protein-engineering.conferenceseries.com">Induced fit</a>” hypothesis were present for enzyme specificity. Here, we have proposed a novel strategy, employed by SCS in <em>Blastocystis</em> for discriminating between cognate and non-cognate ligands (ATP>P). Charged, solvent exposed residues at the entrance to substrate binding site (Gatekeeper residues), produce electrostatic dipole interactions with approaching substrates, and control their access by a novel mechanism called <em>“<a href="https://protein-engineering.conferenceseries.com">Electrostatic Gatekeeper Effect</a>”</em>. In this proof-of-concept study we have demonstrated that nucleotide specificity of wild ATP-specific (K<sub>m</sub>=145±47µM) SCS with positive gatekeepers(KK), can be engineered by altering electrostatic properties of its gatekeeper residues. Our enzyme kinetics results showed dual specificity [ATP(K<sub>m</sub>=230±34µM) & GTP(K<sub>m</sub>=143±17µM)] for gatekeeper mutant(ED) with negative gatekeepers(ED), which favored GTP access to binding site. However, nucleotide binding site mutant(LF) showed no GTP-specificity despite previously reported GTP-supporting residues(LF), and remained ATP-specific (K<sub>m</sub>=265±50µM), because positive gatekeepers(KK) still precluded GTP access to binding site. Interestingly, combining gatekeeper mutant with nucleotide binding site mutant(ED+LF), resulted in exclusive GTP-specificity (K<sub>m</sub>=82±12µM) and no detectable ATP-activity. This striking result was entirely due to; negatively charged gatekeeper residues(ED) favored GTP access, while nucleotide binding site residues(LF) altered ATP binding. These results were further supported by <a href="https://protein-engineering.conferenceseries.com">molecular </a><a href="https://protein-engineering.conferenceseries.com">modelling</a> and simulation studies. Hence it is imperative to explore this strategy in different range of crucial enzymes (synthetases, kinases, transferases) to engineer substrate specificity for various industrial applications and substrate based drug design.</p> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/aso-bakr-mohammed-sulaimanyah-university-iraq" >Aso Bakr Mohammed</a></h4> <p>Sulaimanyah university, Iraq</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/protein-purification" >Protein purification</a> </h6> <p>Time : <b>15:50-16:20</b></p> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Aso-Bakr-Mohammed-47537.jpg" alt="Speaker" title="Aso Bakr Mohammed" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><p style="text-align: justify;"> I  have  completed bachelor at the age of  28 years from Sulaimanyah  university college of science biology department . I work as medical laboratory technologist  at the big hospital named shar hospital. I have puplished two paper .  I am young  to the research area  i will have plan to search and publish more papers .the reason to attend in the conferece to get more experience for tmy future works. <br />  </p> </p> <h5>Abstract:</h5> <p><div style="text-align: justify;"> In this study the preparation of several <a href="https://protein-engineering.conferenceseries.com">agarose</a> and polyacrylamide bead derivatives useful inside the purification of proteins by affinity <a href="https://protein-engineering.conferenceseries.com">chromatography</a> is described. Th ey enable (1) the attachment of <a href="https://protein-engineering.conferenceseries.com">ligands </a>for the gel through extended hydrocarbon chains which place the ligand at different distances within the gel matrix backbone (2) the <a href="https://protein-engineering.conferenceseries.com">covalent attachment</a> of ligands to agarose or polyacrylamide gels through amino, carboxyl, phenolic, or imidazole groups from the ligand and (3) the preparation of adsorbents which contains ligands attached by bonds which are more likely to specifi c chemical cleavage, thus offering method of detaching the intact protein-ligand complex within the affinity adsorbent. It's proven that effective utilization of affinity chromatography oft entimes will critically depend on placing the ligand inside a considerable distance within the matrix backbone. Techniques may also be described that offer important approaches and factors inside the insolubilization of <a href="https://protein-engineering.conferenceseries.com">peptides</a> and <a href="https://protein-engineering.conferenceseries.com">proteins</a> to agarose and polyacrylamide.</div> </p> </div> </div> </div> </section> <section> <div class="col-md-12"> <div class="affiliation bs-callout col-md-12"> <h4><a style="color:#63a7f4;" href="https://protein-engineering.conferenceseries.com/speaker/2016/othman-ahmed-sulaimanyah-university-iraq" >Othman Ahmed</a></h4> <p>Sulaimanyah University, Iraq</p> <h6>Title: <a style="color:#63a7f4" href="https://protein-engineering.conferenceseries.com/abstract/2016/virus-engineering" >Virus engineering</a> </h6> <p>Time : <b>16:20-16:50</b></p> </div> </div> <div class="speaker-bio-abs"> <div class="bio-main"> <img src="https://d2cax41o7ahm5l.cloudfront.net/cs/speaker-photo/Genetic-&-Protein-Engineering-2016-Othman-Ahmed-48720.jpg" alt="Speaker" title="Othman Ahmed" class="img-responsive thumbnail pull-left"> <div class="bio"> <h5>Biography:</h5> <p><div style="text-align: justify;"> I have completed bachelor at the age of 26 years from Sulaimanyah university college of science biology department. I work as biological laboratory technologist at the hospital named shahid aso hospital. I have puplished a paper. I am young to the research area i will have plan to search and publish more papers .the reason to attend in the conferece to get more experience for my future works.</div> </p> <h5>Abstract:</h5> <p><div style="text-align: justify;"> We describe a way to introduce site-specific mutations to the genome of Autographa californica nuclear polyhedrosis virus. Particularly, the A.<a href="https://protein-engineering.conferenceseries.com"> </a><a href="https://protein-engineering.conferenceseries.com">californica</a> nuclear polyhedrosis virus gene for polyhedrin, the primary protein that forms viral occlusions in infected cells, was mutagenized by presenting deletions to the cloned DNA fragment which contains the gene. The mutagenized polyhedrin gene was utilized within the intact viral DNA by mixing fragment and viral DNAs, cotransfecting Spodoptera frugiperda cells, and screening for viral recombinants which in fact had been through <a href="https://protein-engineering.conferenceseries.com">allelic</a><a href="https://protein-engineering.conferenceseries.com"> exchange</a>. <a href="https://protein-engineering.conferenceseries.com">Recombinant infections</a> with mutant polyhedrin genes were acquired by selecting the progeny virus that did not produce viral occlusions in infected cells (occlusion-negative mutants). Analyses of occlusion-negative mutants proven the polyhedrin gene wasn't needed</div> <div style="text-align: justify;"> for creating <a href="https://protein-engineering.conferenceseries.com">infectious</a> virus which deletion of certain sequences within the gene did not modify the control, or decrease the quantity of expression, of polyhedrin. An early on viral <a href="https://protein-engineering.conferenceseries.com">protein</a> of 22,000 molecular weight was apparently not needed for virus replication in vitro, since the synthesis from the protein wasn't detected in cells have been infected with a mutant virus.</div> </p> </div> </div> </div> </section> </div> </article> </div> </div> </section> </div>  <hr /> <link href="https://d2cax41o7ahm5l.cloudfront.net/cs/css/sprite.css" rel="stylesheet" /> <link href='https://fonts.googleapis.com/css?family=Alegreya+Sans:400,700' rel='stylesheet' type='text/css'> <link href="https://www.conferenceseries.com/css/conf_custom.css" rel="stylesheet" /> <div class="col-md-12 text-center bannerObjects"> <h2>Conference Series Destinations</h2> </div> <div class="conference-category-contact-main"> <div class="clearfix conference-category"> <div class="col-md-12"> <div class="row conference-category-sub"> <div class="col-md-4 clearfix" style="padding-right:0px;"> <div 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Scientific Program | Genetic and Protein Engineering 2016 | Biochemistry Conferences | USA | Worldwide Events | Europe | Canada | UK | 2016