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. 1999 Feb;13(2):181-5.
doi: 10.1023/A:1008387715167.

Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure

A Mittermaier  1 , L E Kay, J D Forman-Kay
Affiliations

Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure

A Mittermaier et al. J Biomol NMR. 1999 Feb.

Abstract

Methyl axis (S2axis) and backbone NH (S2NH) order parameters derived from eight proteins have been analyzed. Similar distribution profiles for Ala S2axis and S2NH order parameters were observed. A good correlation between the two S2axis values of Val and Leu methyl groups is noted, although differences between order parameters can arise. The relation of S2axis or S2NH to solvent accessibility and packing density has also been investigated. Correlations are weak, likely reflecting the importance of collective, non-local motions in proteins. The lack of correlation between these simple structural parameters and dynamics emphasizes the importance of motional studies to fully characterize proteins.

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