Detection and characterization of a folding intermediate in barnase by NMR.

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.

journal_name

Nature

journal_title

Nature

authors

Bycroft M,Matouschek A,Kellis JT Jr,Serrano L,Fersht AR

doi

10.1038/346488a0

subject

Has Abstract

pub_date

1990-08-02 00:00:00

pages

488-90

issue

6283

eissn

0028-0836

issn

1476-4687

journal_volume

346

pub_type

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