Publication date: 27 January 2015 Source:Biophysical Journal, Volume 108, Issue 2, Supplement 1
Author(s): Vignesh Kasinath , Kyle W. Harpole , Veronica R. Moorman , Kathleen G. Valentine , Kendra K. Frederick , Kim A. Sharp , Joshua Wand
[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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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
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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...
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11-19-2010 08:32 PM
[NMR paper] Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Biochim Biophys Acta. 1997 Mar 15;1334(2-3):117-22
Authors: Yoshida T, Tanaka M, Mori Y, Ueda I
An obvious difficulty of the study of binding of volatile anesthetics to proteins is to prevent loss of the ligand during the procedure. A novel NMR tube was designed that...
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08-22-2010 03:31 PM
[NMR paper] Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Biochim Biophys Acta. 1997 Mar 15;1334(2-3):117-22
Authors: Yoshida T, Tanaka M, Mori Y, Ueda I
An obvious difficulty of the study of binding of volatile anesthetics to proteins is to prevent loss of the ligand during the procedure. A novel NMR tube was designed that...
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08-22-2010 03:03 PM
[NMR paper] Contributions to conformational entropy arising from bond vector fluctuations measure
Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.
J Mol Biol. 1996 Oct 25;263(2):369-82
Authors: Yang D, Kay LE
The relation between order parameters derived from NMR...
Motion and Conformational Entropy in Protein Function: Creation of an NMR-Based Entropy Meter
Linear Mode
