Thread: NMR paper Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
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Default Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

Related Articles Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

FEBS Lett. 1998 Feb 13;423(1):110-2

Authors: Killick TR, Freund SM, Fersht AR

The folding and unfolding of proteins is generally assumed to be so co-operative that the overall process may be followed by a single probe, such as tryptophan fluorescence. Folding kinetics of three mutants of barnase and chymotrypsin inhibitor 2 (CI2) were studied by real-time NMR. Rate constants for changes in individual residues during the unfolding or refolding of the mutants studied by real-time NMR are all within experimental error of the overall process of folding/unfolding measured by stopped-flow measurements of tryptophan fluorescence. Folding of these mutants is thus highly co-operative. Changes in the tryptophan fluorescence give accurate measurements of the protein folding process.

PMID: 9506851 [PubMed - indexed for MEDLINE]



Source: PubMed
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