Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 70, Issue 1, Pages 1-9Publisher
SPRINGER
DOI: 10.1007/s10858-017-0155-0
Keywords
Protein dynamics; Relaxation dispersion; Extreme CPMG; Conformational exchange; mu s-ms dynamics
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Funding
- James Graham Brown Foundation
- National Center for Research Resources [CoBRE 1P30GM106396]
- Max Planck Society
- EU (ERC) [233227]
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Molecular dynamics play a significant role in how molecules perform their function. A critical method that provides information on dynamics, at the atomic level, is NMR-based relaxation dispersion (RD) experiments. RD experiments have been utilized for understanding multiple biological processes occurring at micro-to-millisecond time, such as enzyme catalysis, molecular recognition, ligand binding and protein folding. Here, we applied the recently developed high-power RD concept to the Carr-Purcell-Meiboom-Gill sequence (extreme CPMG; E-CPMG) for the simultaneous detection of fast and slow dynamics. Using a fast folding protein, gpW, we have shown that previously inaccessible kinetics can be accessed with the improved precision and efficiency of the measurement by using this experiment.
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