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Updated: Jun 10, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure
A Mittermaier1, L E Kay, J D Forman-Kay
1Hospital for Sick Children, Structural Biology and Biochemistry Programme, 555 University Avenue, Toronto, ON, Canada, M5G1X8.
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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