| Issue |
Europhys. Lett.
Volume 42, Number 5, June 1998
|
|
|---|---|---|
| Page(s) | 577 - 581 | |
| Section | Cross-disciplinary physics and related areas of science and technology | |
| DOI | https://doi.org/10.1209/epl/i1998-00290-6 | |
| Published online | 01 September 2002 | |
Folding time of ideal β sheets vs. chain length
Department of Applied Physics, Chalmers University of
Technology S-412 96 Göteborg, Sweden
Boreskov Institute of Catalysis, Russian Academy of Sciences
Novosibirsk 630090, Russia
Received:
25
August
1997
Accepted:
3
April
1998
We present the results of 3D lattice Monte Carlo simulations
of protein folding in the framework of a model taking into account
the dependence of the energy of interaction of amino acid residues
on their orientation and the rigidity of the polypeptide chain.
For the model parameters corresponding to the formation of ideal β
sheets (such flat fragments of proteins are stabilized by hydrogen
bonds), the folding time of chains of length n is found to scale as 
with 
.
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) / 64.60.Cn – Order-disorder transformations; statistical mechanics of model systems
© EDP Sciences, 1998
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