Monitoring conformational dynamics with solid-state R 1rho experiments.
A new application of solid-state rotating frame (R(1rho)) relaxation experiments to observe conformational dynamics is presented. Studies on a model compound, dimethyl sulfone (DMS), show that R(1rho) 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.
Quinn
Caitlin M
CM
Department of Chemistry, Columbia University, 3000 Broadway, New York, NY 10027, USA.
McDermott
Ann E
AE
D000409:Alanine / Q000737:chemistry; D016880:Anisotropy; D004121:Dimethyl Sulfoxide / Q000737:chemistry; D008956:Models, Chemical; D008968:Molecular Conformation; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D013450:Sulfones / Q000737:chemistry
D013450:Sulfones; C025910:dimethyl sulfone; D000409:Alanine; D004121:Dimethyl Sulfoxide