Mean first passage time analysis reveals rate-limiting steps, parallel pathways and dead ends in a simple model of protein folding

Mille Micheelsen; Christian Rischel; Jesper Ferkinghoff-Borg; Raphael Guerois; Luis Serrano

doi:10.1209/epl/i2003-00165-4

Mean first passage time analysis reveals rate-limiting steps, parallel pathways and dead ends in a simple model of protein folding

Mille Micheelsen, Christian Rischel, Jesper Ferkinghoff-Borg, Raphael Guerois, Luis Serrano

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

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

Original language	English
Journal	EPL
Volume	61
Issue number	4
Pages (from-to)	561-566
ISSN	0295-5075
DOIs	https://doi.org/10.1209/epl/i2003-00165-4
Publication status	Published - 2003
Externally published	Yes

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title = "Mean first passage time analysis reveals rate-limiting steps, parallel pathways and dead ends in a simple model of protein folding",

abstract = "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",

author = "Mille Micheelsen and Christian Rischel and Jesper Ferkinghoff-Borg and Raphael Guerois and Luis Serrano",

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T1 - Mean first passage time analysis reveals rate-limiting steps, parallel pathways and dead ends in a simple model of protein folding

AU - Micheelsen, Mille

AU - Rischel, Christian

AU - Ferkinghoff-Borg, Jesper

AU - Guerois, Raphael

AU - Serrano, Luis

PY - 2003

Y1 - 2003

N2 - 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

AB - 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

U2 - 10.1209/epl/i2003-00165-4

DO - 10.1209/epl/i2003-00165-4

M3 - Journal article

SN - 0295-5075

VL - 61

SP - 561

EP - 566

JO - EPL

JF - EPL

IS - 4

ER -

Mean first passage time analysis reveals rate-limiting steps, parallel pathways and dead ends in a simple model of protein folding

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