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Nuclear magnetic resonance measurements of slow conformational dynamics in macromolecules.

作者信息

Lane A N, Lefèvre J F

机构信息

Laboratory of Molecular Structure, National Institute for Medical Research, Mill Hill, London, United Kingdom.

出版信息

Methods Enzymol. 1994;239:596-619. doi: 10.1016/s0076-6879(94)39023-1.

DOI:10.1016/s0076-6879(94)39023-1
PMID:7830600
Abstract

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.

摘要

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