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 i...

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Veröffentlicht in:	Current opinion in structural biology 1997-10, Vol.7 (5), p.732-737
1. Verfasser:	Palmer, Arthur G
Format:	Artikel
Sprache:	eng
Schlagworte:	Carbon Isotopes Catalysis Deuterium Diffusion Ligands Magnetic Resonance Spectroscopy - methods Membrane Proteins - chemistry Nitrogen Isotopes Protein Conformation Proteins - chemistry Proteins - metabolism
Online-Zugang:	Volltext
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Beschreibung
Zusammenfassung:	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.
ISSN:	0959-440X 1879-033X
DOI:	10.1016/S0959-440X(97)80085-1