Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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Probing Protein Side Chain Dynamics Via 13C NMR Relaxation

Author(s): Daiwen Yang

Affiliation: Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543.

Keywords: Protein side chain, relaxation, cross-correlated relaxation, internal motion, dynamics, NMR, 13C relaxation of methine, methylene, 13C relaxation, Carr-Purcell-Meiboom-Gill (CPMG), HSQC, µs-ms timescales, TROSY, NOEs, INEPT, IFABPProtein side chain, relaxation, cross-correlated relaxation, internal motion, dynamics, NMR, 13C relaxation of methine, methylene, 13C relaxation, Carr-Purcell-Meiboom-Gill (CPMG), HSQC, µs-ms timescales, TROSY, NOEs, INEPT, IFABP

Abstract:

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, 13C relaxation of methine, methylene and methyl groups with and without 1H 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 13C autorelaxation and cross-correlated relaxation data are presented too. Finally, recent progress in the use of 13C relaxation to probe the dynamics of protein side chains is detailed mainly for the dynamics of non-deuterated proteins on picosecondnanosecond timescales.

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Article Details

VOLUME: 18
ISSUE: 4
Page: [380 - 395]
Pages: 16
DOI: 10.2174/092986611794653932