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Titlebook: Computational Methods in Protein Evolution; Tobias Sikosek Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019 ph

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發(fā)表于 2025-3-21 19:22:13 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Computational Methods in Protein Evolution
編輯Tobias Sikosek
視頻videohttp://file.papertrans.cn/233/232775/232775.mp4
概述Includes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Computational Methods in Protein Evolution;  Tobias Sikosek Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019 ph
描述.This volume presents a diverse collection of methodologies used to study various problems at the protein sequence and structure level. The chapters in this book look at issues ranging from broad concepts like protein space to specifics like antibody modeling. Topics include point mutations, gene duplication, .de novo. emergence of new genes, pairwise correlated mutations, ancestral protein reconstruction, homology modelling, protein stability and dynamics, and protein-protein interactions. The book also covers a wide range of computational approaches, including sequence and structure alignments, phylogenies, physics-based and mathematical approaches, machine learning, and more. Written in the highly successful .Methods in Molecular Biology. series format, chapters include introductions to their respective topics, lists of the necessary materials and prerequisites, step-by-step, readily reproducible computational protocols (using command line or graphical user interfaces, sometimes including computer code), and tips on troubleshooting and avoiding known pitfalls..Cutting-edge and authoritative, .Computational Methods in Protein Evolution. is a valuable resource that offers useful w
出版日期Book 2019
關(guān)鍵詞phylogenetic trees; sequence reconstruction; co-evolution; Epistasis; allostery
版次1
doihttps://doi.org/10.1007/978-1-4939-8736-8
isbn_softcover978-1-4939-9378-9
isbn_ebook978-1-4939-8736-8Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC, part of Springer Nature 2019
The information of publication is updating

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發(fā)表于 2025-3-21 20:26:16 | 只看該作者
2.3.2.5 Presentation of results,ns. In this chapter we cover the basic theoretical concepts important for the use of calculations utilizing the non-equilibrium alchemical switching methodology. We further provide a detailed step-by-step protocol for estimating the effect of a single amino acid mutation on protein thermostability.
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發(fā)表于 2025-3-22 04:11:58 | 只看該作者
2.2.1.2.3 Continental heat flow literature,ecular functions to genomes through molecular adaptation is one important goal in comparative genomics. In large gene families, however, characterizing adaptation and neofunctionalization across species is challenging, as models have traditionally quantified the timing of duplications without consid
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2.2.1.2.6-7 References for 2.2.1.2,mation about unique intramolecular interactions and, therefore, can assist in the elucidation of biomolecular conformations. It is based on the idea that compensatory mutations at specific residue positions in a sequence help preserve stability of protein architecture and function and leave a statis
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2.2.1.2.4 Continental heat flow results,e, and fitness in biological systems. The applications cover many areas of biological research, including biochemistry, genomics, protein and systems engineering, medicine, and evolutionary biology. However, the quantitative definitions of epistasis vary among fields, and the analysis beyond just pa
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2.2.1.2.4 Continental heat flow results, ASR is the computation of a phylogenetic tree whose leaves are the chosen extant sequences. Most often, the reconstructed sequence related to the root of this tree is of greatest interest: It represents the common ancestor (CA) of the sequences under study. If this sequence encodes a protein, one c
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發(fā)表于 2025-3-23 06:43:50 | 只看該作者
2.2.1.2.6-7 References for 2.2.1.2,re may be strongly conserved despite large divergences in sequence, structural information can be used to help identify homology in such cases..While there exist well-studied models of sequence evolution, structurally informed alignment methods have typically made use of geometric measures of deviat
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