Abstract:
:The folding pathway of the small α/β protein GB1 has been extensively studied during the past two decades using both theoretical and experimental approaches. These studies provided a consensus view that the protein folds in a two-state manner. Here, we reassessed the folding of GB1, both by experiments and simulations, and detected the presence of an on-pathway intermediate. This intermediate has eluded earlier experimental characterization and is distinct from the collapsed state previously identified using ultrarapid mixing. Failure to identify the presence of an intermediate affects some of the conclusions that have been drawn for GB1, a popular model for protein folding studies.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Morrone A,Giri R,Toofanny RD,Travaglini-Allocatelli C,Brunori M,Daggett V,Gianni Sdoi
10.1016/j.bpj.2011.09.013subject
Has Abstractpub_date
2011-10-19 00:00:00pages
2053-60issue
8eissn
0006-3495issn
1542-0086pii
S0006-3495(11)01071-Xjournal_volume
101pub_type
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