| Issue |
Europhys. Lett.
Volume 61, Number 4, February 2003
|
|
|---|---|---|
| Page(s) | 561 - 566 | |
| Section | Interdisciplinary physics and related areas of science and technology | |
| DOI | https://doi.org/10.1209/epl/i2003-00165-4 | |
| Published online | 01 February 2003 | |
Mean first-passage time analysis reveals rate-limiting steps, parallel pathways and dead ends in a simple model of protein folding
1
Complexity Lab., Niels Bohr Institute, University of Copenhagen Blegdamsvej 17, DK-2100 København Ø, Denmark
2
Department of Mathematics and Physics Royal Veterinary and Agricultural University Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark
3
EMBL Heidelberg - Meyerhofstrasse 1, D-69117 Heidelberg, Germany
Corresponding author: rischel@nbi.dk
Received:
2
July
2002
Accepted:
9
December
2002
We have analyzed dynamics on the complex free-energy landscape of protein folding in the FOLD-X model, by calculating for each state of the system the mean first-passage time to the folded state. The resulting kinetic map of the folding process shows that it proceeds in jumps between well-defined, local free-energy minima. Closer analysis of the different local minima allows us to reveal secondary, parallel pathways as well as dead ends.
PACS: 87.15.Aa – Theory and modeling; computer simulation / 82.20.Fd – Collision theories; trajectory models
© EDP Sciences, 2003
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