Protein conformational dynamics dictate the binding affinity for aligand

Collection with item attached
2014
Item details URL
http://open-repository.kisti.re.kr/cube/handle/open_repository/483711.do
DOI
10.1038/ncomms4724
Title
Protein conformational dynamics dictate the binding affinity for aligand
Description
This work was supported by the Pioneer Research Program for ConvergingTechnology (2008-2000218) of the Ministry of Science, ICT and FuturePlanning, and Brain Korea 21 of the Ministry of Education to H.-S.K.,and by Creative Research Initiatives (20090081562) and the WCU Programof the National Research Foundation of Korea to S.H.
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.
provenance
Made available in Cube on 2018-09-28T14:54:08Z (GMT). No. of bitstreams: 0
language
English
author
Seo, Moon-Hyeong
Park, Jeongbin
Kim, Eunkyung
Hohng, Sungchul
Kim, Hak-Sung
orcid
Park, Jeongbin/0000-0002-9064-4912
accessioned
2018-09-28T14:54:08Z
available
2018-09-28T14:54:08Z
issued
2014
citation
NATURE COMMUNICATIONS(5)
issn
2041-1723
uri
http://open-repository.kisti.re.kr/cube/handle/open_repository/483711.do
Funder
교육부
Funding Program
BK21플러스사업(0.5)
Project ID
1345228877
Jurisdiction
Rep.of Korea
Project Name
BK21 PLUS BioKAIST Initiative
rights
openAccess
type
article


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