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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Seo MH,Park J,Kim E,Hohng S,Kim HSdoi
10.1038/ncomms4724subject
Has Abstractpub_date
2014-04-24 00:00:00pages
3724issn
2041-1723pii
ncomms4724journal_volume
5pub_type
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