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Three-helix-bundle protein in a Ramachandran model

Irbäck, A LU ; Sjunnesson, F LU and Wallin, S LU (2000) In Proceedings of the National Academy of Sciences 97(25). p.8-13614
Abstract

We study the thermodynamic behavior of a model protein with 54 amino acids that forms a three-helix bundle in its native state. The model contains three types of amino acids and five to six atoms per amino acid and has the Ramachandran torsional angles phi(i), psi(i) as its degrees of freedom. The force field is based on hydrogen bonds and effective hydrophobicity forces. For a suitable choice of the relative strength of these interactions, we find that the three-helix-bundle protein undergoes an abrupt folding transition from an expanded state to the native state. Also shown is that the corresponding one- and two-helix segments are less stable than the three-helix sequence.

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author
organization
publishing date
type
Contribution to journal
publication status
published
keywords
Models, Molecular, Protein Conformation, Proteins, Thermodynamics
in
Proceedings of the National Academy of Sciences
volume
97
issue
25
pages
5 pages
publisher
National Academy of Sciences
external identifiers
  • Scopus:0034610275
ISSN
0027-8424
DOI
10.1073/pnas.240245297
language
English
LU publication?
yes
id
3454bf29-d051-4659-a8e9-d7ee673af5c1
date added to LUP
2016-08-17 16:27:42
date last changed
2016-12-04 04:53:21
@misc{3454bf29-d051-4659-a8e9-d7ee673af5c1,
  abstract     = {<p>We study the thermodynamic behavior of a model protein with 54 amino acids that forms a three-helix bundle in its native state. The model contains three types of amino acids and five to six atoms per amino acid and has the Ramachandran torsional angles phi(i), psi(i) as its degrees of freedom. The force field is based on hydrogen bonds and effective hydrophobicity forces. For a suitable choice of the relative strength of these interactions, we find that the three-helix-bundle protein undergoes an abrupt folding transition from an expanded state to the native state. Also shown is that the corresponding one- and two-helix segments are less stable than the three-helix sequence.</p>},
  author       = {Irbäck, A and Sjunnesson, F and Wallin, S},
  issn         = {0027-8424},
  keyword      = {Models, Molecular,Protein Conformation,Proteins,Thermodynamics},
  language     = {eng},
  month        = {12},
  number       = {25},
  pages        = {8--13614},
  publisher    = {ARRAY(0xd75faa0)},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {Three-helix-bundle protein in a Ramachandran model},
  url          = {http://dx.doi.org/10.1073/pnas.240245297},
  volume       = {97},
  year         = {2000},
}