Protein conformational dynamics dictate the binding affinity for a ligand

Moon-Hyeong Seo, Jeongbin Park, Eunkyung Kim, Sungchul Hohng and Hak-Sung Kim ()
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Moon-Hyeong Seo: Korea Advanced Institute of Science and Technology
Jeongbin Park: Seoul National University
Eunkyung Kim: Korea Advanced Institute of Science and Technology
Sungchul Hohng: Seoul National University
Hak-Sung Kim: Korea Advanced Institute of Science and Technology

Nature Communications, 2014, vol. 5, issue 1, 1-7

Abstract: Abstract Interactions between a protein and a ligand are essential to all biological processes. Binding and dissociation are the two fundamental steps of ligand–protein interactions, and determine the binding affinity. Intrinsic conformational dynamics of proteins have been suggested to play crucial roles in ligand binding and dissociation. Here, we demonstrate how protein dynamics dictate the binding and dissociation of a ligand through a single-molecule kinetic analysis for a series of maltose-binding protein mutants that have different intrinsic conformational dynamics and dissociation constants for maltose. Our results provide direct evidence that the ligand dissociation is determined by the intrinsic opening rate of the protein.

Date: 2014
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DOI: 10.1038/ncomms4724

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