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) |
|---|---|
| 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