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• W2414685952 abstract "Abstract Previous experimental study measuring the binding affinities of biotin to the wild type streptavidin (WT) and three mutants (S45A, D128A and S45A/D128A double mutant) has shown that the loss of binding affinity from the double mutation is larger than the direct sum of those from two single mutations. The origin of this cooperativity has been investigated in this work through molecular dynamics simulations and the end-state free energy method using the polarized protein-specific charge. The results show that this cooperativity comes from both the enthalpy and entropy contributions. The former contribution mainly comes from the alternations of solvation free energy. Decomposition analysis shows that the mutated residues nearly have no contributions to the cooperativity. Instead, N49 and S88, which are located at the entry of the binding pocket and interact with the carboxyl group of biotin, make the dominant contribution among all the residues in the first binding shell around biotin." @default.
• W2414685952 created "2016-06-24" @default.
• W2414685952 creator A5004123133 @default.
• W2414685952 creator A5037829735 @default.
• W2414685952 creator A5045389074 @default.
• W2414685952 date "2016-06-01" @default.
• W2414685952 modified "2023-10-12" @default.
• W2414685952 title "The origin of the cooperativity in the streptavidin-biotin system: A computational investigation through molecular dynamics simulations" @default.
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• W2414685952 doi "https://doi.org/10.1038/srep27190" @default.
• W2414685952 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4888747" @default.
• W2414685952 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27249234" @default.
• W2414685952 hasPublicationYear "2016" @default.
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