Format

Send to

Choose Destination
J Magn Reson. 2014 Apr;241:3-17. doi: 10.1016/j.jmr.2014.01.008.

Chemical exchange in biomacromolecules: past, present, and future.

Author information

1
Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, New York, NY 10032, United States. Electronic address: agp6@columbia.edu.

Abstract

The perspective reviews quantitative investigations of chemical exchange phenomena in proteins and other biological macromolecules using NMR spectroscopy, particularly relaxation dispersion methods. The emphasis is on techniques and applications that quantify the populations, interconversion kinetics, and structural features of sparsely populated conformational states in equilibrium with a highly populated ground state. Applications to folding, molecular recognition, catalysis, and allostery by proteins and nucleic acids are highlighted.

KEYWORDS:

Dynamics; Kinetics; NMR; Nucleic acids; Proteins; Relaxation

PMID:
24656076
PMCID:
PMC4049312
DOI:
10.1016/j.jmr.2014.01.008
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center