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Titlebook: Docking Screens for Drug Discovery; Walter Filgueira de Azevedo Jr. Book 2019 Springer Science+Business Media, LLC, part of Springer Natur

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书目名称Docking Screens for Drug Discovery
编辑Walter Filgueira de Azevedo Jr.
视频video
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: Docking Screens for Drug Discovery;  Walter Filgueira de Azevedo Jr. Book 2019 Springer Science+Business Media, LLC, part of Springer Natur
描述This book focuses on recent developments in docking simulations for target proteins with chapters on specific techniques or applications for docking simulations, including the major docking programs. Additionally, the volume explores the scoring functions developed for the analysis of docking results and to predict ligand-binding affinity as well as the importance of docking simulations for the initial stages of drug discovery. Written for the highly successful .Methods in Molecular Biology. series, this collection presents the kind of detail and key implementation advice to ensure successful results. .Authoritative and practical, .Docking Screens for Drug Discovery. aims to serve those interested in molecular docking simulation and also in the application of these methodologies for drug discovery..
出版日期Book 2019
关键词Drug discovery; Protein-ligand docking simulations; Scoring functions; Molecular docking simulation; Com
版次1
doihttps://doi.org/10.1007/978-1-4939-9752-7
isbn_softcover978-1-4939-9754-1
isbn_ebook978-1-4939-9752-7Series 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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Alex Austin,Martina Fischer,Norbert Ropersr Waals interactions relevant to molecular recognition of a ligand by the binding pocket of a protein target. We describe the Lennard-Jones potential and its application to calculate potential energy for an ensemble of structures to highlight the main features related to the importance of this interaction for binding affinity.
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