[NMR paper] Microsecond motions probed by near-rotary-resonance R1?15N MAS NMR experiments: the model case of protein overall-rocking in crystals.
Microsecond motions probed by near-rotary-resonance R1?15N MAS NMR experiments: the model case of protein overall-rocking in crystals.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Microsecond motions probed by near-rotary-resonance R1?15N MAS NMR experiments: the model case of protein overall-rocking in crystals.
J Biomol NMR. 2018 May 30;:
Authors: Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K
Abstract
...
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05-31-2018 11:07 PM
Microsecond motions probed by near-rotary-resonance R 1Ï? 15 N MAS NMR experiments: the model case of protein overall-rocking in crystals
Microsecond motions probed by near-rotary-resonance R 1Ï? 15 N MAS NMR experiments: the model case of protein overall-rocking in crystals
Abstract
Solid-state near-rotary-resonance measurements of the spinâ??lattice relaxation rate in the rotating frame (R1Ï?) is a powerful NMR technique for studying molecular dynamics in the microsecond time scale. The small difference between the spin-lock (SL) and magic-angle-spinning (MAS) frequencies allows sampling very slow motions, at the same time it brings up some methodological challenges. In this work,...
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05-30-2018 08:10 AM
[NMR paper] NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
J Phys Chem B. 2013 May 2;
Authors: Xia J, Deng NJ, Levy RM
Abstract
Calculating NMR relaxation effects for proteins with dynamics on multiple timescales generally requires very long trajectories based on conventional molecular dynamics simulations. In this report,...
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05-04-2013 09:18 PM
Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation
Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation
Justin L. Lorieau, John M. Louis and Ad Bax
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2045309/aop/images/medium/ja-2011-045309_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2045309
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/2aIqfWmdIn4
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Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation.
Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation.
Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation.
J Am Chem Soc. 2011 Aug 17;
Authors: Lorieau JL, Louis JM, Bax A
Abstract
Biological membranes present a highly fluid environment and integration of proteins within such membranes is itself highly dynamic: proteins diffuse laterally within the plane of the membrane, and rotationally about the normal vector of this plane. We...
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08-19-2011 02:56 PM
[NMR paper] Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid s
Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy.
Related Articles Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy.
J Mol Biol. 2002 Nov 8;323(5):899-907
Authors: Stumber M, Geyer M, Graf R, Kalbitzer HR, Scheffzek K, Haeberlen U
The folding, structure and biological function of many proteins are inherently dynamic properties of the protein molecule. Often, the respective molecular processes are preserved upon protein...
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11-24-2010 08:58 PM
[NMR paper] NMR 15N relaxation and structural studies reveal slow conformational exchange in bars
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
J Mol Biol. 1997 May 2;268(2):494-511
Authors: Wong KB, Fersht AR, Freund SM
Barstar an 89-residue protein consisting of four helices and a three-stranded parallel beta-sheet, is the intracellular inhibitor of the...
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08-22-2010 03:31 PM
[NMR paper] NMR 15N relaxation and structural studies reveal slow conformational exchange in bars
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
J Mol Biol. 1997 May 2;268(2):494-511
Authors: Wong KB, Fersht AR, Freund SM
Barstar an 89-residue protein consisting of four helices and a three-stranded parallel beta-sheet, is the intracellular inhibitor of the...
Slow conformational exchange and overall rocking motion in ubiquitin protein crystals - Nature.com
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