4.3 Article

Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments

Journal

JOURNAL OF BIOMOLECULAR NMR
Volume 70, Issue 1, Pages 1-9

Publisher

SPRINGER
DOI: 10.1007/s10858-017-0155-0

Keywords

Protein dynamics; Relaxation dispersion; Extreme CPMG; Conformational exchange; mu s-ms dynamics

Funding

  1. James Graham Brown Foundation
  2. National Center for Research Resources [CoBRE 1P30GM106396]
  3. Max Planck Society
  4. EU (ERC) [233227]

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.3
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available