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. 1990 Aug 2;346(6283):488-90.
doi: 10.1038/346488a0.

Detection and characterization of a folding intermediate in barnase by NMR

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Detection and characterization of a folding intermediate in barnase by NMR

M Bycroft et al. Nature. .

Abstract

Protein engineering is being developed for mapping the energetics and pathway of protein folding. From kinetic studies on wild-type and mutant proteins, the sequence and energetics of formation of tertiary interactions of side chains can be mapped and the formation of secondary structure inferred. Here we cross-check and complement results from this approach by using a recently developed procedure that traps and characterizes secondary structure in intermediate states using 1H NMR. The refolding of barnase is shown to be a multiphasic process in which the secondary structure in alpha-helices and beta-sheets and some turns is formed more rapidly than is the overall folding.

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