Microscopic insights into the NMR relaxation based protein conformational entropy meter.
J Am Chem Soc. 2013 Sep 6;
Authors: Kasinath V, Sharp KA, Wand AJ
Abstract
Conformational entropy is a potentially important thermodynamic parameter contributing to protein function. Quantitative measures of conformational entropy are necessary for an understanding of its role but have been difficult to obtain. An empirical method that utilizes changes in conformational dynamics as a proxy for changes in conformational entropy has recently been introduced. Here we probe the microscopic origins of the link between conformational dynamics and conformational entropy using molecular dynamics simulations. Simulation of seven proteins gave an excellent correlation with measures of side-chain motion derived from NMR relaxation. The simulations show that the motion of methyl-bearing side-chains are sufficiently coupled to that of other side chains to serve as excellent reporters of the overall side-chain conformational entropy. These results tend to validate the use of ex-perimentally accessible measures of methyl motion - the NMR-derived generalized order parameters - as a proxy from which to derive changes in protein conformational entropy.
PMID: 24007504 [PubMed - as supplied by publisher]
The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation
The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation
Available online 13 December 2012
Publication year: 2012
Source:Current Opinion in Structural Biology</br>
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Microscopic insights into the NMR relaxation based protein conformational entropy meter.
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