期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 44, 期 -, 页码 31-38出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2016.10.016
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资金
- Department of Science and Technology, India
- Ministry of Human Resource and Development
Protein-protein interactions mediate several cellular functions, which can be understood from the information obtained using the three-dimensional structures of protein-protein complexes and binding affinity data. This review focuses on computational aspects of predicting the best native-like complex structure and binding affinities. The first part covers the prediction of protein-protein complex structures and the advantages of conformational searching and scoring functions in protein protein docking. The second part is devoted to various aspects of protein-protein interaction thermodynamics, such as databases for binding affinities and other thermodynamic parameters, computational methods to predict the binding affinity using either the three-dimensional structures of complexes or amino acid sequences, and change in binding affinities of the complexes upon mutations. We provide the latest developments on protein-protein docking and binding affinity studies along with a list of available computational resources for understanding protein-protein interactions.
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