Publication date: 28 January 2014 Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1
Author(s): Marc S. Hoemberger , Christopher G. Wilson , Dorothee Kern
[NMR paper] Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Acc Chem Res. 2013 Feb 13;
Authors: Yan S, Suiter CL, Hou G, Zhang H, Polenova T
Abstract
In living organisms, biological molecules often organize into multicomponent complexes. Such assemblies consist of various proteins and carry out essential functions, ranging from cell division, transport, and energy transduction to catalysis, signaling, and viral...
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Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Protein Pept Lett. 2011 Jan 11;
Authors: Yang D
Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, (13)C relaxation of methine, methylene and methyl groups with and without...
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01-13-2011 12:00 PM
[NMR paper] Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations.
Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations.
Related Articles Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations.
Biophys J. 2005 Sep;89(3):2113-20
Authors: Heise H, Luca S, de Groot BL, Grubmüller H, Baldus M
An approach is introduced to characterize conformational ensembles of intrinsically unstructured peptides on the atomic level using two-dimensional solid-state NMR data and...
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12-01-2010 06:56 PM
[NMR paper] Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin r
Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
Related Articles Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
J Am Chem Soc. 2005 Jun 8;127(22):8214-25
Authors: Tugarinov V, Ollerenshaw JE, Kay LE
New NMR experiments for the measurement of side-chain dynamics in high molecular weight ( approximately 100 kDa) proteins are presented. The experiments quantify (2)H spin...
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11-25-2010 08:21 PM
[NMR paper] Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 vi
Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 via 15N rotating frame NMR relaxation measurements: biological implications.
Related Articles Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 via 15N rotating frame NMR relaxation measurements: biological implications.
Biochemistry. 1998 Sep 1;37(35):12320-30
Authors: Banci L, Bertini I, Cavazza C, Felli IC, Koulougliotis D
Rotating frame 15N relaxation NMR experiments have been performed to study the local mobility of the...
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11-17-2010 11:15 PM
Probing Microsecond Time Scale Dynamics in Proteins by Methyl 1H Carr-Purcell-Meiboom
Probing Microsecond Time Scale Dynamics in Proteins by Methyl 1H Carr-Purcell-Meiboom-Gill Relaxation Dispersion NMR Measurements. Application to Activation of the Signaling Protein NtrCr
Renee Otten, Janice Villali, Dorothee Kern and Frans A. A. Mulder
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107410x/aop/images/medium/ja-2010-07410x_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107410x
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/aNQDkVtDj-4
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11-17-2010 06:08 PM
Probing Microsecond Time Scale Dynamics in Proteins by Methyl (1)H Carr-Purcell-Meibo
Probing Microsecond Time Scale Dynamics in Proteins by Methyl (1)H Carr-Purcell-Meiboom-Gill Relaxation Dispersion NMR Measurements. Application to Activation of the Signaling Protein NtrC(r).
Probing Microsecond Time Scale Dynamics in Proteins by Methyl (1)H Carr-Purcell-Meiboom-Gill Relaxation Dispersion NMR Measurements. Application to Activation of the Signaling Protein NtrC(r).
J Am Chem Soc. 2010 Nov 8;
Authors: Otten R, Villali J, Kern D, Mulder FA
To study microsecond processes by relaxation dispersion NMR spectroscopy, low power...
Probing an Ancient Protein's Dynamics with NMR
Linear Mode
