Nuclear magnetic resonance measurements of slow conformational dynamics in macromolecules.

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.

journal_name

Methods Enzymol

journal_title

Methods in enzymology

authors

Lane AN,Lefèvre JF

doi

10.1016/s0076-6879(94)39023-1

subject

Has Abstract

pub_date

1994-01-01 00:00:00

pages

596-619

eissn

0076-6879

issn

1557-7988

pii

S0076-6879(94)39023-1

journal_volume

239

pub_type

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