Nuclear magnetic resonance measurements of slow conformational dynamics in macromolecules.
The combined use of rotating-frame relaxation methods, temperature-dependent measurements of line shapes and magnetization transfer experiments allows in favorable cases the examination in some detail of exchange processes that occur on the millisecond time scale. It is possible to determine not only the rate constants, but also the activation parameters and chemical shifts even for events that are in fast exchange on the chemical shift time scale. Such measurements complement the information obtainable from heteronuclear relaxation methods that probe mainly the fast librational motions in macromolecules and may provide information important for functional studies of biological macromolecules.
Lane
A N
AN
Laboratory of Molecular Structure, National Institute for Medical Research, Mill Hill, London, United Kingdom.
Lefèvre
J F
JF
D000595:Amino Acid Sequence; D001483:Base Sequence; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry; D011487:Protein Conformation; D013816:Thermodynamics
D046911:Macromolecular Substances; D009838:Oligodeoxyribonucleotides; D009842:Oligopeptides