Abstract：
:Applications of sensitive new technologies, in particular, two-dimensional NMR spectroscopy, have allowed detection of folded structures in short peptide fragments of proteins in aqueous solution under conditions where native proteins fold. These structures are in rapid dynamic exchange with unfolded states. These observations provide evidence in support of models for protein folding which postulate localized regions of folded structure as initiation sites for the folding process. Since these initiation processes are expected to be rapid, such models are consistent with kinetic evidence that the rate-determining steps of protein folding occur late in the process and probably involve rearrangement of incorrectly folded intermediates.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Wright PE,Dyson HJ,Lerner RAdoi
10.1021/bi00419a001subject
Has Abstractpub_date
1988-09-20 00:00:00pages
7167-75issue
19eissn
0006-2960issn
1520-4995journal_volume
27pub_type
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