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Probing Protein Side Chain Dynamics Via 13C NMR Relaxation

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

Document Type: Research Article

Publication date: 2011-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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