[NMR paper] SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy.
SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy.
Related Articles SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy.
J Phys Chem B. 2021 Jan 15;:
Authors: Mendelman N, Meirovitch E
Abstract
We report on amide (N-H) NMR relaxation from the protein S100A1 analyzed with the slowly relaxing local structure (SRLS) approach. S100A1 comprises two...
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01-16-2021 04:55 PM
[NMR paper] Conformational Entropy from NMR Relaxation in Proteins: the SRLS Perspective.
Conformational Entropy from NMR Relaxation in Proteins: the SRLS Perspective.
Related Articles Conformational Entropy from NMR Relaxation in Proteins: the SRLS Perspective.
J Phys Chem B. 2017 Jan 06;:
Authors: Tchaicheeyan O, Meirovitch E
Abstract
Conformational entropy changes associated with bond-vector motions in proteins contribute to the free energy of ligand binding. To derive such contributions we apply the slowly relaxing local structure (SRLS) approach to NMR relaxation from (15)N-H bonds or C-CDH2 moieties of several...
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01-07-2017 01:27 PM
Motion and Conformational Entropy in Protein Function: Creation of an NMR-Based Entropy Meter
Motion and Conformational Entropy in Protein Function: Creation of an NMR-Based Entropy Meter
Publication date: 27 January 2015
Source:Biophysical Journal, Volume 108, Issue 2, Supplement 1</br>
Author(s): Vignesh Kasinath , Kyle W. Harpole , Veronica R. Moorman , Kathleen G. Valentine , Kendra K. Frederick , Kim A. Sharp , Joshua Wand</br>
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01-28-2015 05:28 PM
[NMR paper] Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Proc Natl Acad Sci U S A. 2014 Oct 13;
Authors: Baxa MC, Haddadian EJ, Jumper JM, Freed KF, Sosnick TR
Abstract
The loss of conformational entropy is a major contribution in the thermodynamics of protein folding. However, accurate determination of the quantity...
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10-15-2014 10:58 AM
MicroscopicInsights into the NMR Relaxation-BasedProtein Conformational Entropy Meter
MicroscopicInsights into the NMR Relaxation-BasedProtein Conformational Entropy Meter
Vignesh Kasinath, Kim A. Sharp and A. Joshua Wand
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja405200u/aop/images/medium/ja-2013-05200u_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja405200u
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Oa6aJARKKwg
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09-25-2013 11:34 PM
[NMR paper] Microscopic insights into the NMR relaxation based protein conformational entropy meter.
Microscopic insights into the NMR relaxation based protein conformational entropy meter.
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...
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09-07-2013 09:54 PM
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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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...
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02-03-2013 10:13 AM
[NMR paper] NMR relaxation studies of the role of conformational entropy in protein stability and
NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Related Articles NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Acc Chem Res. 2001 May;34(5):379-88
Authors: Stone MJ
Recent advances in the measurement and analysis of protein NMR relaxation data have made it possible to characterize the dynamical properties of many backbone and side chain groups. With certain caveats, changes in flexibility that occur upon ligand binding, mutation, or...
Protein conformational entropy is not slaved to water - Nature.com
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