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Titlebook: Identification of Ligand Binding Site and Protein-Protein Interaction Area; Irena Roterman-Konieczna Book 2013 Springer Science+Business M

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書目名稱Identification of Ligand Binding Site and Protein-Protein Interaction Area
編輯Irena Roterman-Konieczna
視頻videohttp://file.papertrans.cn/461/460837/460837.mp4
概述Comparative analysis of models based on geometry versus those based on knowledge of the biological phenomenon Application note Relation to biological phenomena.All illustrations in full color.A review
叢書名稱Focus on Structural Biology
圖書封面Titlebook: Identification of Ligand Binding Site and Protein-Protein Interaction Area;  Irena Roterman-Konieczna Book 2013 Springer Science+Business M
描述This volume presents a review of the latest numerical techniques used to identify ligand binding and protein complexation sites. It should be noted that there are many other theoretical studies devoted to predicting the activity of specific proteins and that useful protein data can be found in numerous databases. The aim of advanced computational techniques is to identify the active sites in specific proteins and moreover to suggest a generalized mechanism by which such protein-ligand (or protein-protein) interactions can be effected. Developing such tools is not an easy task – it requires extensive expertise in the area of molecular biology as well as a firm grasp of numerical modeling methods. Thus, it is often viewed as a prime candidate for interdisciplinary research.
出版日期Book 2013
關鍵詞bioinformatics; ligand binding; protein-protein complexation; structure of proteins
版次1
doihttps://doi.org/10.1007/978-94-007-5285-6
isbn_softcover978-94-017-8284-5
isbn_ebook978-94-007-5285-6Series ISSN 1571-4853 Series E-ISSN 2542-9566
issn_series 1571-4853
copyrightSpringer Science+Business Media Dordrecht 2013
The information of publication is updating

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Can the Structure of the Hydrophobic Core Determine the Complexation Site?,ophobic interactions (Levitt 1976) were not particularly successful, even though the influence of the aqueous environment on molecular dynamics cannot be underestimated in respect to experimental observations.
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Prediction of Protein-Protein Binding Interfaces,ire temporary binding of cofactors (e.g. regulation of transcription factors (Huxford et al. 1998)), or are part of complicated protein machinery (e.g. proton-driven rotors in ATP synthases (Boyer 1997; Oster and Wang 1999, 2003)).
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Docking Predictions of Protein-Protein Interactions and Their Assessment: The CAPRI Experiment,the mode of association between proteins of known structure. Since 2001, the performance of docking procedures has been assessed in blind predictions by the CAPRI (Critical Assessment of PRedicted Interactions) experiment. The results show that docking routinely yields good models of the protein-pro
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