Related ArticlesA simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
J Magn Reson. 1998 Feb;130(2):329-34
Authors: Daragan VA, Mayo KH
A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational amplitudes, and rotational correlation coefficients with different NMR relaxation parameters have been obtained. Auto- and cross-correlation spectral densities are considered, and it is shown that proton-coupled 13C NMR relaxation measurements allow detailed motional information to be obtained.
Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain 1H Probes
Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain 1H Probes
Alexandar L. Hansen, Patrik Lundstrom, Algirdas Velyvis and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210711v/aop/images/medium/ja-2011-10711v_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210711v
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/jaMjjnA_QTw
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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...
[NMR paper] What contributions to protein side-chain dynamics are probed by NMR experiments? A mo
What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
Related Articles What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
J Mol Biol. 2005 May 27;349(1):185-203
Authors: Best RB, Clarke J, Karplus M
Molecular dynamics simulations of the structurally homologous proteins TNfn3 and FNfn10 have been used to investigate the contributions to side-chain dynamics measured by NMR relaxation experiments. The...
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[NMR paper] Characterization of threonine side chain dynamics in an antifreeze protein using natu
Characterization of threonine side chain dynamics in an antifreeze protein using natural abundance 13C NMR spectroscopy.
Related Articles Characterization of threonine side chain dynamics in an antifreeze protein using natural abundance 13C NMR spectroscopy.
J Biomol NMR. 2004 Jun;29(2):139-50
Authors: Daley ME, Sykes BD
The dynamics of threonine side chains of the Tenebrio molitor antifreeze protein (TmAFP) were investigated using natural abundance (13)C NMR. In TmAFP, the array of threonine residues on one face of the protein is responsible...
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[NMR paper] Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study
Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.
Related Articles Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.
J Am Chem Soc. 2003 Feb 19;125(7):1748-58
Authors: Choy WY, Shortle D, Kay LE
NMR relaxation data on disordered proteins can provide insight into both structural and dynamic properties of these molecules. Because of chemical shift degeneracy in correlation spectra, detailed site-specific analyses of side chain dynamics...
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[NMR paper] Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studi
Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Related Articles Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Biochemistry. 2001 Jun 5;40(22):6559-69
Authors: Flynn PF, Bieber Urbauer RJ, Zhang H, Lee AL, Wand AJ
A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is...
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Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analy
Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analysis of Human Vinexin SH3 Domain using a Genetically Encoded (15)N/(19)F-Labeled Unnatural Amino Acid.
Related Articles Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analysis of Human Vinexin SH3 Domain using a Genetically Encoded (15)N/(19)F-Labeled Unnatural Amino Acid.
Biochem Biophys Res Commun. 2010 Oct 11;
Authors: Shi P, Xi Z, Wang H, Shi C, Xiong Y, Tian C
SH3 is a ubiquitous domain mediating protein-protein interactions....
A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation da
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