Volume 61, Number 4, February 2003
|Page(s)||561 - 566|
|Section||Interdisciplinary physics and related areas of science and technology|
|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
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: firstname.lastname@example.org
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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