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Protein Allostery and Conformational Dynamics.

Title: Protein Allostery and Conformational Dynamics.
Name(s): Guo, Jingjing, author
Zhou, Huan-Xiang, author
Type of Resource: text
Genre: Journal Article
Date Issued: 2016-06-08
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: The functions of many proteins are regulated through allostery, whereby effector binding at a distal site changes the functional activity (e.g., substrate binding affinity or catalytic efficiency) at the active site. Most allosteric studies have focused on thermodynamic properties, in particular, substrate binding affinity. Changes in substrate binding affinity by allosteric effectors have generally been thought to be mediated by conformational transitions of the proteins or, alternatively, by changes in the broadness of the free energy basin of the protein conformational state without shifting the basin minimum position. When effector binding changes the free energy landscape of a protein in conformational space, the change affects not only thermodynamic properties but also dynamic properties, including the amplitudes of motions on different time scales and rates of conformational transitions. Here we assess the roles of conformational dynamics in allosteric regulation. Two cases are highlighted where NMR spectroscopy and molecular dynamics simulation have been used as complementary approaches to identify residues possibly involved in allosteric communication. Perspectives on contentious issues, for example, the relationship between picosecond-nanosecond local and microsecond-millisecond conformational exchange dynamics, are presented.
Identifier: FSU_pmch_26876046 (IID), 10.1021/acs.chemrev.5b00590 (DOI), PMC5011433 (PMCID), 26876046 (RID), 26876046 (EID)
Grant Number: R01 GM058187
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at
Subject(s): Allosteric Regulation
Catalytic Domain
Molecular Dynamics Simulation
NIMA-Interacting Peptidylprolyl Isomerase/chemistry
NIMA-Interacting Peptidylprolyl Isomerase/metabolism
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Protein Conformation
Persistent Link to This Record:
Host Institution: FSU
Is Part Of: Chemical reviews.
Issue: iss. 11, vol. 116

Choose the citation style.
Guo, J., & Zhou, H. -X. (2016). Protein Allostery and Conformational Dynamics. Chemical Reviews. Retrieved from