Protein folding in the absence of a clear free-energy barrier
Irbäck, Anders LU
(2003)
In Acta Physica Polonica. Series B: Elementary Particle Physics, Nuclear Physics, Statistical Physics, Theory of Relativity, Field Theory
34(10).
p.4867-4878
- Abstract
- Many small proteins fold in a two-state manner, the rate-limiting step being the passage of the free-energy barrier separating the unfolded state from the native one. The free-energy barrier is, however, weak or absent for the fastest-folding proteins. Here a simple diffusion picture for such proteins is discussed. It is tested on a model protein that makes a three-helix bundle. Assuming the motion along individual reaction coordinates to be diffusive on timescales beyond the reconfiguration time for a single helix, it is found that the relaxation time can be predicted within a factor of two. It is also shown that melting curves for this protein to a good approximation can be described in terms of a simple two-state system, despite the... (More)
- Many small proteins fold in a two-state manner, the rate-limiting step being the passage of the free-energy barrier separating the unfolded state from the native one. The free-energy barrier is, however, weak or absent for the fastest-folding proteins. Here a simple diffusion picture for such proteins is discussed. It is tested on a model protein that makes a three-helix bundle. Assuming the motion along individual reaction coordinates to be diffusive on timescales beyond the reconfiguration time for a single helix, it is found that the relaxation time can be predicted within a factor of two. It is also shown that melting curves for this protein to a good approximation can be described in terms of a simple two-state system, despite the absence of a clear free-energy barrier. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/296364
- author
- Irbäck, Anders
LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Acta Physica Polonica. Series B: Elementary Particle Physics, Nuclear Physics, Statistical Physics, Theory of Relativity, Field Theory
- volume
- 34
- issue
- 10
- pages
- 4867 - 4878
- publisher
- Jagiellonian University, Cracow, Poland
- external identifiers
-
- wos:000186418300016
- scopus:18244414276
- ISSN
- 0587-4254
- language
- English
- LU publication?
- yes
- id
- aab5c547-4dec-4160-9214-f6241228c4ed (old id 296364)
- alternative location
- http://th-www.if.uj.edu.pl/acta/vol34/abs/v34p4867.htm
- date added to LUP
- 2016-04-01 15:28:45
- date last changed
- 2022-12-12 04:36:53
@article{aab5c547-4dec-4160-9214-f6241228c4ed,
abstract = {{Many small proteins fold in a two-state manner, the rate-limiting step being the passage of the free-energy barrier separating the unfolded state from the native one. The free-energy barrier is, however, weak or absent for the fastest-folding proteins. Here a simple diffusion picture for such proteins is discussed. It is tested on a model protein that makes a three-helix bundle. Assuming the motion along individual reaction coordinates to be diffusive on timescales beyond the reconfiguration time for a single helix, it is found that the relaxation time can be predicted within a factor of two. It is also shown that melting curves for this protein to a good approximation can be described in terms of a simple two-state system, despite the absence of a clear free-energy barrier.}},
author = {{Irbäck, Anders}},
issn = {{0587-4254}},
language = {{eng}},
number = {{10}},
pages = {{4867--4878}},
publisher = {{Jagiellonian University, Cracow, Poland}},
series = {{Acta Physica Polonica. Series B: Elementary Particle Physics, Nuclear Physics, Statistical Physics, Theory of Relativity, Field Theory}},
title = {{Protein folding in the absence of a clear free-energy barrier}},
url = {{http://th-www.if.uj.edu.pl/acta/vol34/abs/v34p4867.htm}},
volume = {{34}},
year = {{2003}},
}