Two-state folding over a weak free-energy barrier
Författare
Summary, in English
We present a Monte Carlo study of a model protein with 54 amino acids that folds directly to its native three-helix-bundle state without forming any well-defined intermediate state. The free-energy barrier separating the native and unfolded states of this protein is found to be weak, even at the folding temperature. Nevertheless, we find that melting curves to a good approximation can be described in terms of a simple two-state system, and that the relaxation behavior is close to single exponential. The motion along individual reaction coordinates is roughly diffusive on timescales beyond the reconfiguration time for a single helix. A simple estimate based on diffusion in a square-well potential predicts the relaxation time within a factor of two.
Publiceringsår
2003
Språk
Engelska
Sidor
1457-1465
Publikation/Tidskrift/Serie
Biophysical Journal
Volym
85
Issue
3
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
Cell Press
Ämne
- Biophysics
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1542-0086