Probing molecular motion by NMR.
Recently developed solution NMR methods for measuring 2H, 13C, and 15N spin relaxation, coupled with biosynthetic isotopic enrichment, permit the characterization of backbone and sidechain dynamical properties of proteins on picosecond/nanosecond and microsecond/millisecond timescales. Theoretical interpretations of the relaxation data provide insights into the biophysical and functional properties of proteins.
Palmer
A G
AG
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. agp6@columbia.edu
D002247:Carbon Isotopes; D002384:Catalysis; D003903:Deuterium; D004058:Diffusion; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry; D009587:Nitrogen Isotopes; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D002247:Carbon Isotopes; D008024:Ligands; D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D011506:Proteins; D003903:Deuterium