A simple method to measure protein side-chain mobility using NMR chemical shifts.
 

A simple method to measure protein side-chain mobility using NMR chemical shifts.

http://www.bionmr.com//www.ncbi.nlm....ed-acspubs.jpg Related Articles A simple method to measure protein side-chain mobility using NMR chemical shifts.

J Am Chem Soc. 2013 Sep 13;

Authors: Berjanskii MV, Wishart DS

Abstract
Protein side-chain motions are involved in many important biological processes including enzymatic catalysis, allosteric regulation, and the mediation of protein-protein, protein-DNA, protein-RNA, and protein-cofactor interactions. NMR spectroscopy has long been used to provide insights into the motions of side-chain groups. Currently, the method of choice for studying side-chain dynamics by NMR is the measurement of methyl 2H auto-relaxation. Methyl 2H auto-relaxation exhibits simple relaxation mechanisms and can be straightforwardly converted to meaningful dynamic parameters. However, methyl groups can only be found in 6 of 19 side-chain bearing amino acids. Consequently, only a sparse assessment of protein side-chain dynamics is possible. Therefore, there is a significant interest in developing novel methods of studying side-chain motions that can be applied to all types of side-chains. Here, we show how side-chain chemical shifts can be used to determine the magnitude of fast side-chain motions in proteins. The chemical shift method is applicable to all side-chain bearing residues and does not require any additional measurements beyond standard NMR experiments for backbone and side-chain assignments.


PMID: 24032347 [PubMed - as supplied by publisher]



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