Abstract
Hydrogen exchange experiments under slow exchange conditions show that an omega loop in cytochrome c (residues 40-57) acts as a cooperative unfolding/refolding unit under native conditions. This unit behavior accounts for an initial step on the unfolding pathway, a final step in refolding, and a number of other structural, functional and evolutionary properties.
Original language | English (US) |
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Pages (from-to) | 29-36 |
Number of pages | 8 |
Journal | Journal of Molecular Biology |
Volume | 331 |
Issue number | 1 |
DOIs | |
State | Published - Aug 1 2003 |
Bibliographical note
Funding Information:This work was supported by research grants from the NIH and the Mathers Foundation.
Keywords
- Cytochrome c
- Hydrogen exchange
- Omega loop
- Protein folding
- Protein function