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
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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
[NMR paper] Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
Related Articles Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
J Biol Chem. 2013 May 3;
Authors: Esposito G, Garvey M, Alverdi V, Pettirossi F, Corazza A, Fogolari F, Polano M, Mangione PP, Giorgetti S, Stoppini M, Rekas A, Bellotti V, Heck AJ, Carver JA...
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05-07-2013 01:30 PM
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
Abstract The combination of the wide availability of protein backbone and side-chain NMR chemical shifts with advances in understanding of their relationship to protein structure makes these parameters useful for the assessment of structural-dynamic protein models. A new chemical shift predictor (PPM) is introduced, which is solely based on physicalâ??chemical contributions to the chemical shifts for both the protein backbone and methyl-bearing amino-acid side chains. To...
[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] 13C-NMR relaxation study on mobility of the DNA-binding arm of HU.
13C-NMR relaxation study on mobility of the DNA-binding arm of HU.
Related Articles 13C-NMR relaxation study on mobility of the DNA-binding arm of HU.
J Biochem. 1994 Nov;116(5):1153-5
Authors: Kakuta Y, Hojo H, Aimoto S, Tanaka I, Hikichi K
The mobility of the DNA-binding arm of HU protein was studied by 13C-NMR spectroscopy. The correlation times tau c of Phe47C alpha in the body and Gly60C alpha in the arm of HU were determined for HU and HU-DNA complex. The value of tau c of Phe47C alpha is 2-4 times larger than that of Gly60C alpha...
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08-22-2010 03:29 AM
[NMR paper] Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on huma
Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.
Related Articles Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.
Biochemistry. 1992 Nov 3;31(43):10431-7
Authors: Redfield C, Boyd J, Smith LJ, Smith RA, Dobson CM
15N NOE, T1, and T2 measurements have been carried out on uniformly 15N-labeled human interleukin-4. Analysis of the results in terms of order parameters (S2) shows that although the helical core of this four-helix-bundle protein...