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 (1)H decoupling are described briefly for a better understanding of how spin relaxation is associated with motional (dynamics) parameters. Developments in the measurement and interpretation of (13)C auto-relaxation and cross-correlated relaxation data are presented too. Finally, recent progress in the use of (13)C relaxation to probe the dynamics of protein side chains is detailed mainly for the dynamics of non-deuterated proteins on picoseconds-nanosecond timescales.
PMID: 21222636 [PubMed - as supplied by publisher]
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
nmrlearner
Journal club
0
02-03-2012 09:50 AM
[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...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[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...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[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...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[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...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-cor
A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
Related Articles A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
J Mol Biol. 1998 Mar 13;276(5):939-54
Authors: Yang D, Mittermaier A, Mok YK, Kay LE
Two new NMR experiments are presented for measuring side-chain dynamics in proteins. The first method, requiring 15N, 13C,...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation da
A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
Related Articles A 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...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
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....