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Journal of Biomolecular NMR

, Volume 45, Issue 1–2, pp 5–8 | Cite as

Monitoring conformational dynamics with solid-state R experiments

  • Caitlin M. Quinn
  • Ann E. McDermott
Communication

Abstract

A new application of solid-state rotating frame (R ) relaxation experiments to observe conformational dynamics is presented. Studies on a model compound, dimethyl sulfone (DMS), show that R relaxation due to reorientation of a chemical shift anisotropy (CSA) tensor undergoing chemical exchange can be used to monitor slow-to-intermediate timescale conformational exchange processes. Control experiments used d 6 -DMS and alanine to confirm that the technique is monitoring reorientation of the CSA tensor rather than dipolar interactions or methyl group rotation. The application of this method to proteins could represent a new site-specific probe of conformational dynamics.

Keywords

Rotating frame relaxation Chemical shift anisotropy Molecular dynamics Chemical exchange Dimethyl sulfone 

Supplementary material

10858_2009_9346_MOESM1_ESM.doc (94 kb)
Supplementary material 1 (DOC 93 kb)

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Copyright information

© Springer Science+Business Media B.V. 2009

Authors and Affiliations

  1. 1.Department of ChemistryColumbia UniversityNew YorkUSA

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