Abstract：
:The hydrogen exchange behavior of a four-helix bundle protein in low concentrations of denaturant reveals some partially unfolded forms that are significantly more stable than the fully unfolded state. Kinetic folding of the protein, however, is apparently two-state in the absence of the accumulation of early folding intermediates. The partially unfolded forms are either as folded as or more folded than the rate-limiting transition state and appear to represent the major intermediates in a folding and unfolding reaction. These results are consistent with the suggestion that partially unfolded intermediates may form after the rate-limiting step for small proteins with apparent two-state folding kinetics.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Chu R,Pei W,Takei J,Bai Ydoi
10.1021/bi025872nsubject
Has Abstractpub_date
2002-06-25 00:00:00pages
7998-8003issue
25eissn
0006-2960issn
1520-4995pii
bi025872njournal_volume
41pub_type
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