Abstract
A recent study of experimental results for flavodoxin-like folds suggests that proteins from this family may exhibit a similar, signature pattern of folding intermediates. We study the folding landscapes of three proteins from the flavodoxin family (CheY, apoflavodoxin, and cutinase) using a simple nucleation and growth model that accurately describes both experimental and simulation results for the transition state structure, and the structure of on-pathway and misfolded intermediates for CheY. Although the landscape features of these proteins agree in basic ways with the results of the study, the simulations exhibit a range of folding behaviours consistent with two alternate folding routes corresponding to nucleation and growth from either side of the central β-strand.
Original language | English (US) |
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Pages (from-to) | 646-653 |
Number of pages | 8 |
Journal | Journal of Molecular Biology |
Volume | 358 |
Issue number | 3 |
DOIs | |
State | Published - May 5 2006 |
Keywords
- equilibrium intermediates
- fold families
- non-native interactions
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology