Two-state folding over a weak free-energy barrier
(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
- 2024-02-24 10:30:20
@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}}, }