| Issue |
Europhys. Lett.
Volume 35, Number 8, September II 1996
|
|
|---|---|---|
| Page(s) | 627 - 632 | |
| Section | Cross-disciplinary physics and related areas of science and technology | |
| DOI | https://doi.org/10.1209/epl/i1996-00162-1 | |
| Published online | 01 September 2002 | |
A criterion that determines fast folding of proteins: A model study
1
Facultad de
Física, P. Universidad Católica de Chile - Casilla 306, Santiago
22, Chile
2
Institute for Physical Science and Technology, University of
Maryland, College Park, MD 20742, USA
Received:
8
March
1996
Accepted:
23
July
1996
We consider the statistical mechanics of a full set of
two-dimensional protein-like
heteropolymers, whose
thermodynamics is characterized by the
coil-to-globular (
) and the folding (Tf) transition
temperatures. For our model, the typical time scale for reaching
the unique native conformation is shown to scale as
.
We argue that Tf scales
linearly with the inverse of entropy of low-energy non-native states,
whereas is almost
independent of it. As 
, non-productive
intermediates decrease, and the initial rapid collapse of
the protein leads to structures resembling the
native state.
Based solely on thermodynamic information,
σ can be used to predict sequences that fold rapidly.
PACS: 87.10.+e – General, theoretical, and mathematical biophysics (including logic of biosystems, quantum biology, and relevant aspects of thermodynamics, information theory, cybernetics, and bionics) / 05.70.Fh – Phase transitions: general aspects / 64.60.Cn – Order-disorder and statistical mechanics of model systems
© EDP Sciences, 1996
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