Available online 13 December 2012
Publication year: 2012 Source:Current Opinion in Structural Biology
Historically it has been virtually impossible to experimentally determine the contribution of residual protein entropy to fundamental protein activities such as the binding of ligands. Recent progress has illuminated the possibility of employing NMR relaxation methods to quantitatively determine the role of changes in conformational entropy in molecular recognition by proteins. The method rests on using fast internal protein dynamics as a proxy. Initial results reveal a large and variable role for conformational entropy in the binding of ligands by proteins. Such a role for conformational entropy in molecular recognition has significant implications for enzymology, signal transduction, allosteric regulation and the development of protein-directed pharmaceuticals. Graphical abstract
Highlights
? Fast motion interconverts states with significant conformational entropy. ? Fast internal motion can be characterized in a site resolved way using solution NMR relaxation phenomena. ? Internal protein motion can be used as a proxy for conformational entropy. ? Conformational entropy can contribute significantly to ligand binding by proteins.
Heteronuclear Adiabatic Relaxation Dispersion (HARD) for Quantitative Analysis of Conformational Dynamics in Proteins
Heteronuclear Adiabatic Relaxation Dispersion (HARD) for Quantitative Analysis of Conformational Dynamics in Proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Nathaniel J. Traaseth, Fa-An Chao, Larry R. Masterson, Silvia Mangia, Michael Garwood, Shalom Michaeli, Burckhard Seelig, Gianluigi Veglia</br>
NMR relaxation methods probe biomolecular motions over a wide range of timescales. In particular, the rotating frame spin-lock R1? and Carr-Purcell-Meiboom-Gill (CPMG) R2 experiments are commonly used to characterize ?sec-msec dynamics, which...
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Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Yi Xue, Joshua M. Ward, Tairan Yuwen, Ivan S. Podkorytov and Nikolai R. Skrynnikov
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206442c/aop/images/medium/ja-2011-06442c_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206442c
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Insights into the local residual entropy of proteins provided by NMR relaxation.
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Highlights
Linear Mode
