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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)
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author
organization
publishing date
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
Jagellonian 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
2007-09-13 12:42:18
date last changed
2018-01-07 08:38:23
@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    = {Jagellonian 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},
  volume       = {34},
  year         = {2003},
}