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A minimalistic all-atom approach to protein folding

Irbäck, Anders LU (2003) In Journal of Physics: Condensed Matter1990-01-01+01:00 15(18). p.1797-1807
Abstract
Using simple sequence-based potentials, the folding properties of a designed three-helix-bundle protein, an alpha-helix and a beta-hairpin are studied. The three-helix-bundle protein is modelled using 5-6 atoms per amino acid and is found to undergo a first-order-like folding transition in which chain collapse and helix formation cannot be separated, which is in-accord with experimental data. The other two sequences are studied using a model that contains all atoms and are indeed found to make an alpha-helix and a beta-hairpin, respectively, for exactly the same choice of parameters. The calculated melting curves are, moreover, in reasonable quantitative agreement with experimental data, for both peptides. The melting curves are found to... (More)
Using simple sequence-based potentials, the folding properties of a designed three-helix-bundle protein, an alpha-helix and a beta-hairpin are studied. The three-helix-bundle protein is modelled using 5-6 atoms per amino acid and is found to undergo a first-order-like folding transition in which chain collapse and helix formation cannot be separated, which is in-accord with experimental data. The other two sequences are studied using a model that contains all atoms and are indeed found to make an alpha-helix and a beta-hairpin, respectively, for exactly the same choice of parameters. The calculated melting curves are, moreover, in reasonable quantitative agreement with experimental data, for both peptides. The melting curves are found to be quite well described by a simple two-state model, although the energy distributions lack a clear bimodal shape. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Physics: Condensed Matter1990-01-01+01:00
volume
15
issue
18
pages
1797 - 1807
publisher
IOP Publishing
external identifiers
  • wos:000183133200015
  • scopus:0037846494
ISSN
1361-648X
DOI
10.1088/0953-8984/15/18/313
language
English
LU publication?
yes
id
b2d688fb-869b-4bfa-be2e-ccc61977aa1b (old id 309766)
date added to LUP
2007-08-03 10:38:40
date last changed
2018-01-07 09:39:46
@article{b2d688fb-869b-4bfa-be2e-ccc61977aa1b,
  abstract     = {Using simple sequence-based potentials, the folding properties of a designed three-helix-bundle protein, an alpha-helix and a beta-hairpin are studied. The three-helix-bundle protein is modelled using 5-6 atoms per amino acid and is found to undergo a first-order-like folding transition in which chain collapse and helix formation cannot be separated, which is in-accord with experimental data. The other two sequences are studied using a model that contains all atoms and are indeed found to make an alpha-helix and a beta-hairpin, respectively, for exactly the same choice of parameters. The calculated melting curves are, moreover, in reasonable quantitative agreement with experimental data, for both peptides. The melting curves are found to be quite well described by a simple two-state model, although the energy distributions lack a clear bimodal shape.},
  author       = {Irbäck, Anders},
  issn         = {1361-648X},
  language     = {eng},
  number       = {18},
  pages        = {1797--1807},
  publisher    = {IOP Publishing},
  series       = {Journal of Physics: Condensed Matter1990-01-01+01:00},
  title        = {A minimalistic all-atom approach to protein folding},
  url          = {http://dx.doi.org/10.1088/0953-8984/15/18/313},
  volume       = {15},
  year         = {2003},
}