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Titlebook: Computational Strategies Towards Improved Protein Function Prophecy of Xylanases from Thermomyces la; MVK Karthik,Pratyoosh Shukla Book 20

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發(fā)表于 2025-3-21 16:24:59 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Computational Strategies Towards Improved Protein Function Prophecy of Xylanases from Thermomyces la
編輯MVK Karthik,Pratyoosh Shukla
視頻videohttp://file.papertrans.cn/234/233150/233150.mp4
概述One of the first reports showing stable, energy efficient model towards improved protein function prediction screening in-silico structure based mutagenesis of xylanases from Thermomyces lanuginosus.D
叢書名稱SpringerBriefs in Systems Biology
圖書封面Titlebook: Computational Strategies Towards Improved Protein Function Prophecy of Xylanases from Thermomyces la;  MVK Karthik,Pratyoosh Shukla Book 20
描述This Brief reports on the interplay of an amino-acid mutation towards substrate which could lead to enhanced effects on mutant. These effects need? to? be given consideration in? the? engineering? processes of protein stability and further exploration of such learning are required to provide novel indication for selection of an enzymes.? There? are? very? few? reports? showing? such? stable,? energy? efficient? model? towards? improved? protein function prediction screening in-silico structure based mutagenesis of xylanases from Thermomyces lanuginosus?
出版日期Book 2012
關(guān)鍵詞bioinformatics; enzymes; protein prediction
版次1
doihttps://doi.org/10.1007/978-1-4614-4723-8
isbn_softcover978-1-4614-4722-1
isbn_ebook978-1-4614-4723-8Series ISSN 2193-4746 Series E-ISSN 2193-4754
issn_series 2193-4746
copyrightThe Author(s) 2012
The information of publication is updating

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沙發(fā)
發(fā)表于 2025-3-21 21:52:00 | 只看該作者
板凳
發(fā)表于 2025-3-22 02:27:57 | 只看該作者
https://doi.org/10.1007/978-1-4614-4723-8bioinformatics; enzymes; protein prediction
地板
發(fā)表于 2025-3-22 06:27:35 | 只看該作者
5#
發(fā)表于 2025-3-22 08:59:21 | 只看該作者
6#
發(fā)表于 2025-3-22 13:49:21 | 只看該作者
https://doi.org/10.1007/978-3-662-46924-8 acids, also referred to as residues. To be able to perform their biological function, proteins often fold into one, or more, specific spatial conformations, driven by a number of non-covalent interactions, such as hydrogen bonding, ionic interactions, Van der Waals’ forces, and hydrophobic packing.
7#
發(fā)表于 2025-3-22 19:36:49 | 只看該作者
Alternative Vehicle and Fuel Options, In the present work, diverse binding site residues viz. Trp18, Asn44, Val46, Tyr73, Tyr77, Ala176, Glu178 were studied using SYBYL and it was envisaged that Tyr77 was conserved in family 11 xylanases. Furthermore, during residue conservation analysis through ConSurf method Tyr77 was observed as hig
8#
發(fā)表于 2025-3-22 22:02:00 | 只看該作者
https://doi.org/10.1007/978-3-662-46924-8Computational protein design assists methodical, high-throughput protein and ligand mutagenesis and has been the focus of several researchers in recent years, resulting in significant improvements in methodology and application.
9#
發(fā)表于 2025-3-23 02:51:13 | 只看該作者
10#
發(fā)表于 2025-3-23 06:05:51 | 只看該作者
Alternative Vehicle Market Potential,The identification of a good binding site and characterization of a target protein is a prime importance that leads to its functional annotations. At the outset 37 sequences of various family 11 xylanases were selected for multiple sequence alignment as shown in Fig.?4.1 and found Tyr77 (Y77) to be conserved.
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