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• W2150192011 abstract "Protein-protein recognition plays a central role in most biological processes. Although the structures of many protein-protein complexes have been solved in molecular detail, general rules describing affinity and selectivity of protein-protein interactions do not accurately account for the extremely diverse nature of the interfaces. We investigate the extent to which a simple physical model can account for the wide range of experimentally measured free energy changes brought about by alanine mutation at protein-protein interfaces. The model successfully predicts the results of alanine scanning experiments on globular proteins (743 mutations) and 19 protein-protein interfaces (233 mutations) with average unsigned errors of 0.81 kcal/mol and 1.06 kcal/mol, respectively. The results test our understanding of the dominant contributions to the free energy of protein-protein interactions, can guide experiments aimed at the design of protein interaction inhibitors, and provide a stepping-stone to important applications such as interface redesign." @default.
• W2150192011 created "2016-06-24" @default.
• W2150192011 creator A5000906927 @default.
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• W2150192011 date "2002-10-15" @default.
• W2150192011 modified "2023-10-10" @default.
• W2150192011 title "A simple physical model for binding energy hot spots in protein–protein complexes" @default.
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• W2150192011 doi "https://doi.org/10.1073/pnas.202485799" @default.
• W2150192011 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/137846" @default.
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