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

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Abstract

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 cooperative. Changes in the tryptophan fluorescence give accurate measurements of the protein folding process.

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Killick, T. R., Freund, S. M. V., & Fersht, A. R. (1998). Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2. FEBS Letters, 423(1), 110–112. https://doi.org/10.1016/S0014-5793(98)00075-1

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