ISSN:
1573-5001
Keywords:
Chemical exchange
;
Longitudinal 2-spin-order
;
Protein folding
;
Protein denaturation
;
15N-labeled proteins
;
Conformational equilibrium
;
2D difference NMR spectroscopy
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Summary Observation of the exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment enables studies of slow dynamic processes in biological macromolecules with minimal interference from background signals. The experiment is used to establish relations between corresponding15N−1H groups in the native globular form and an unfolded form of the protein 434 repressor (1–69) present in aqueous solution containing 4.2 M urea.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01874572
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