Abstract
The hydrogen exchange behavior of native cytochrome c in low concentrations of denaturant reveals a sequence of metastable, partially unfolded forms that occupy free energy levels reaching up to the fully unfolded state. The step from one form to another is accomplished by the unfolding of one or more cooperative units of structure. The cooperative units are entire omega loops or mutually stabilizing pairs of whole helices and loops. The partially unfolded forms detected by hydrogen exchange appear to represent the major intermediates in the reversible, dynamic unfolding reactions that occur even at native conditions and thus may define the major pathway for cytochrome c folding.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 27, 2006, 2:19 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 14, 2024, 11:56 p.m.) |
Indexed | 3 weeks, 1 day ago (Aug. 5, 2025, 8:29 a.m.) |
Issued | 30 years, 1 month ago (July 14, 1995) |
Published | 30 years, 1 month ago (July 14, 1995) |
Published Print | 30 years, 1 month ago (July 14, 1995) |
@article{Bai_1995, title={Protein Folding Intermediates: Native-State Hydrogen Exchange}, volume={269}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.7618079}, DOI={10.1126/science.7618079}, number={5221}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Bai, Yawen and Sosnick, Tobin R. and Mayne, Leland and Englander, S. Walter}, year={1995}, month=jul, pages={192–197} }