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Titlebook: Data Mining Techniques for the Life Sciences; Oliviero Carugo,Frank Eisenhaber Book 2016Latest edition Springer Science+Business Media New

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發(fā)表于 2025-3-21 19:32:39 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Data Mining Techniques for the Life Sciences
編輯Oliviero Carugo,Frank Eisenhaber
視頻videohttp://file.papertrans.cn/263/262907/262907.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.Includes supplementary materia
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Data Mining Techniques for the Life Sciences;  Oliviero Carugo,Frank Eisenhaber Book 2016Latest edition Springer Science+Business Media New
描述.This volume details several important databases and data mining tools. .Data Mining Techniques for the Life Sciences, Second Edition .guides readers through archives of macromolecular three-dimensional structures, databases of protein-protein interactions, thermodynamics information on protein and mutant stability, “Kbdock” protein domain structure database, PDB_REDO databank, erroneous sequences, substitution matrices, tools to align RNA sequences, interesting procedures for kinase family/subfamily classifications, new tools to predict protein crystallizability, metabolomics data, drug-target interaction predictions, and a recipe for protein-sequence-based function prediction and its implementation in the latest version of the ANNOTATOR software suite. Written in the highly successful .Methods in Molecular Biology .series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls...Authoritative and cutting-edge,. Data Mining Techniques for the Life Sciences, Second Edition. .aims to ensure successful results in th
出版日期Book 2016Latest edition
關(guān)鍵詞protein-protein interactions; align RNA sequences; thermodynamics; “Kbdock” protein domain structure da
版次2
doihttps://doi.org/10.1007/978-1-4939-3572-7
isbn_softcover978-1-4939-8081-9
isbn_ebook978-1-4939-3572-7Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media New York 2016
The information of publication is updating

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Protein Structure Databasese various atlases that describe each experimentally determined protein structure and provide useful links, analyses, and schematic diagrams relating to its 3D structure and biological function. Also of great interest are the databases that classify 3D structures by their folds as these can reveal ev
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Applications of Protein Thermodynamic Database for Understanding Protein Mutant Stability and Designlly, protein stability is measured with circular dichroism, differential scanning calorimetry, and fluorescence spectroscopy using thermal and denaturant denaturation methods. These experimental data have been accumulated in the form of a database, ProTherm, thermodynamic database for proteins and m
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Classification and Exploration of 3D Protein Domain Interactions Using Kbdocknction and evolutionary relationships. Additionally, structural knowledge of existing domain–domain interactions can provide a useful way to find structural templates with which to model the 3D structures of unsolved protein complexes. Here we present a straightforward guide to using the “Kbdock” pr
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Data Mining of Macromolecular Structuresimization in drug development. Applying data mining techniques on these experimentally determined structures requires a highly uniform, standardized structural data source. The Protein Data Bank (PDB) has evolved over the years toward becoming the standard resource for macromolecular structures. How
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Criteria to Extract High-Quality Protein Data Bank Subsets for Structure Users the subsets are non-redundant and of high quality. The first problem can be solved relatively easily at the sequence level or at the structural level. The second, on the contrary, needs special attention. It is not sufficient, in fact, to consider the crystallographic resolution and other feature m
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