Abstract
Previous results indicate that the folding pathways of cytochrome c and other proteins progressively build the target native protein in a predetermined stepwise manner by the sequential formation and association of native-like foldon units. The present work used native state hydrogen exchange methods to investigate a structural anomaly in cytochrome c results that suggested the concerted folding of two segments that have little structural relationship in the native protein. The results show that the two segments, an 18-residue omega loop and a 10-residue helix, are able to unfold and refold independently, which allows a branch point in the folding pathway. The pathway that emerges assembles native-like foldon units in a linear sequential manner when prior native-like structure can template a single subsequent foldon, and optional pathway branching is seen when prior structure is able to support the folding of two different foldons.
Original language | English (US) |
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Pages (from-to) | 1946-1956 |
Number of pages | 11 |
Journal | Protein Science |
Volume | 16 |
Issue number | 9 |
DOIs | |
State | Published - Sep 2007 |
Keywords
- Cytochrome c
- Foldon
- Partially unfolded form
- Predetermined pathway
- Protein folding
- Sequential stabilization