Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2014 Apr 24;5:3724.
doi: 10.1038/ncomms4724.

Protein Conformational Dynamics Dictate the Binding Affinity for a Ligand

Affiliations

Protein Conformational Dynamics Dictate the Binding Affinity for a Ligand

Moon-Hyeong Seo et al. Nat Commun. .

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.

Similar articles

See all similar articles

Cited by 26 articles

See all "Cited by" articles

Publication types

LinkOut - more resources

Feedback