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
Naturejournal_title
Natureauthors
Bycroft M,Matouschek A,Kellis JT Jr,Serrano L,Fersht ARdoi
10.1038/346488a0subject
Has Abstractpub_date
1990-08-02 00:00:00pages
488-90issue
6283eissn
0028-0836issn
1476-4687journal_volume
346pub_type
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