| Literature DB >> 29188417 |
Jithender G Reddy1,2, Supriya Pratihar1, David Ban3, Sebastian Frischkorn1, Stefan Becker1, Christian Griesinger1, Donghan Lee4.
Abstract
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.Keywords: Conformational exchange; Extreme CPMG; Protein dynamics; Relaxation dispersion; µs–ms dynamics
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Year: 2017 PMID: 29188417 DOI: 10.1007/s10858-017-0155-0
Source DB: PubMed Journal: J Biomol NMR ISSN: 0925-2738 Impact factor: 2.835