Selective characterization of microsecond motions in proteins by NMR relaxation.

ABSTRACT: The three-dimensional structures of macromolecules fluctuate over a wide range of time-scales. Separating the individual dynamic processes according to frequency is of importance in relating protein motions to biological function and stability. We present here a general NMR method for the specific characterization of microsecond motions at backbone positions in proteins even in the presence of other dynamics such as large-amplitude nanosecond motions and millisecond chemical exchange processes. The method is based on measurement of relaxation rates of four bilinear coherences and relies on the ability of strong continuous radio frequency fields to quench millisecond chemical exchange. The utility of the methodology is demonstrated and validated through two specific examples focusing on the

SUBMITTER: Hansen DF 

PROVIDER: S-EPMC7386800 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature