Two-state folding over a weak free-energy barrier
Favrin, Giorgio LU ; Irbäck, Anders LU
; Samuelsson, Björn
LU
and Wallin, Stefan
LU
(2003)
In Biophysical Journal
85(3).
p.1457-1465
- Abstract
- We present a Monte Carlo study of a model protein with 54 amino acids that folds directly to its native three-helix-bundle state without forming any well-defined intermediate state. The free-energy barrier separating the native and unfolded states of this protein is found to be weak, even at the folding temperature. Nevertheless, we find that melting curves to a good approximation can be described in terms of a simple two-state system, and that the relaxation behavior is close to single exponential. The motion along individual reaction coordinates is roughly diffusive on timescales beyond the reconfiguration time for a single helix. A simple estimate based on diffusion in a square-well potential predicts the relaxation time within a factor... (More)
- We present a Monte Carlo study of a model protein with 54 amino acids that folds directly to its native three-helix-bundle state without forming any well-defined intermediate state. The free-energy barrier separating the native and unfolded states of this protein is found to be weak, even at the folding temperature. Nevertheless, we find that melting curves to a good approximation can be described in terms of a simple two-state system, and that the relaxation behavior is close to single exponential. The motion along individual reaction coordinates is roughly diffusive on timescales beyond the reconfiguration time for a single helix. A simple estimate based on diffusion in a square-well potential predicts the relaxation time within a factor of two. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/302318
- author
- Favrin, Giorgio
LU
; Irbäck, Anders
LU
; Samuelsson, Björn
LU
and Wallin, Stefan
LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biophysical Journal
- volume
- 85
- issue
- 3
- pages
- 1457 - 1465
- publisher
- Cell Press
- external identifiers
-
- wos:000185009900010
- scopus:0041821616
- ISSN
- 1542-0086
- language
- English
- LU publication?
- yes
- id
- 60924ccc-1642-427f-ace4-07a32acfecf0 (old id 302318)
- alternative location
- http://www.biophysj.org/cgi/content/abstract/85/3/1457
- date added to LUP
- 2016-04-01 12:29:43
- date last changed
- 2022-12-11 04:49:59
@article{60924ccc-1642-427f-ace4-07a32acfecf0,
abstract = {{We present a Monte Carlo study of a model protein with 54 amino acids that folds directly to its native three-helix-bundle state without forming any well-defined intermediate state. The free-energy barrier separating the native and unfolded states of this protein is found to be weak, even at the folding temperature. Nevertheless, we find that melting curves to a good approximation can be described in terms of a simple two-state system, and that the relaxation behavior is close to single exponential. The motion along individual reaction coordinates is roughly diffusive on timescales beyond the reconfiguration time for a single helix. A simple estimate based on diffusion in a square-well potential predicts the relaxation time within a factor of two.}},
author = {{Favrin, Giorgio and Irbäck, Anders and Samuelsson, Björn and Wallin, Stefan}},
issn = {{1542-0086}},
language = {{eng}},
number = {{3}},
pages = {{1457--1465}},
publisher = {{Cell Press}},
series = {{Biophysical Journal}},
title = {{Two-state folding over a weak free-energy barrier}},
url = {{http://www.biophysj.org/cgi/content/abstract/85/3/1457}},
volume = {{85}},
year = {{2003}},
}