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Titlebook: Protein Supersecondary Structures; Methods and Protocol Alexander E. Kister Book 2025Latest edition The Editor(s) (if applicable) and The A

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发表于 2025-3-21 16:32:58 | 显示全部楼层 |阅读模式
书目名称Protein Supersecondary Structures
副标题Methods and Protocol
编辑Alexander E. Kister
视频videohttp://file.papertrans.cn/765/764658/764658.mp4
概述Includes cutting-edge techniques.Provides step-by-step detail essential for reproducible results.Contains key implementation advice from the experts
丛书名称Methods in Molecular Biology
图书封面Titlebook: Protein Supersecondary Structures; Methods and Protocol Alexander E. Kister Book 2025Latest edition The Editor(s) (if applicable) and The A
描述.This new edition delves into the latest developments in the field and new techniques used to study secondary and supersecondary structures (SSS) in proteins. Beyond the tremendous advances in the field from the AI-based AlphaFold algorithm, researchers continue to untangle how specific structures and protein folds come to be, and these chapters contain numerous techniques to further pursue this study. Written for the highly successful .Methods in Molecular Biology. series, chapters contain the kind of detailed implementation advice needed to ensure effective results in the lab. .. ..Authoritative and practical, .Protein Supersecondary Structures: Methods and Protocols, Third Edition. serves as a valuable resource for researchers exploring the relationship between amino acids sequences and protein structures, the evolution of proteins, and the dynamics of protein formation..
出版日期Book 2025Latest edition
关键词AlphaFold; Artificial intelligence; Deep Learning; Strands and helices; Protein function
版次3
doihttps://doi.org/10.1007/978-1-0716-4213-9
isbn_softcover978-1-0716-4215-3
isbn_ebook978-1-0716-4213-9Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines
The information of publication is updating

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Advances in Prediction of Posttranslational Modification Sites Known to Localize in Protein Supersecondary Structures,mbeddings from protein language models, integration of structural information, utilization of reliable positive and negative sites, and application of contrastive learning. These methodologies and emerging trends offer a roadmap for novel innovations in addressing PTM prediction challenges, particularly those linked to supersecondary structures.
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Mean-Field Coupling Between Local Interactions in Proteins in Relation to Chirality, Secondary, and Supersecondary Structure Formation, and Allostery,residue chirality, and that the improper-torsional potentials that correspond to the coupling between local conformational states of the sites adjacent to a given .-carbon atom enable us to model amino-acid-residue enantiomerization.
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Ig or Not Ig? That Is the Question: The Nucleating Supersecondary Structure of the Ig-Fold and the Extended Ig Universe,gical arrangements. In this chapter, we go through examples of Ig, Ig-like, and Ig-extended domains as in a journey through cells: in the cell nucleus, in the cytoplasm, or on extracellular regions of cell surface receptors, and in viruses.
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Prediction of the Stability of Protein Substructures Using AI/ML Techniques,hods. The findings represent a pivotal step towards the rational design of proteins with tailored properties, offering new insights into protein engineering and the fundamental principles underpinning protein supersecondary structures.
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