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Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

Three-helix-bundle protein in a Ramachandran model

Author

  • A Irbäck
  • F Sjunnesson
  • S Wallin

Summary, in English

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.

Department/s

  • Computational Biology and Biological Physics

Publishing year

2000-12-05

Language

English

Pages

8-13614

Publication/Series

Proceedings of the National Academy of Sciences

Volume

97

Issue

25

Document type

Journal article

Publisher

National Acad Sciences

Keywords

  • Models, Molecular
  • Protein Conformation
  • Proteins
  • Thermodynamics

Status

Published

ISBN/ISSN/Other

  • ISSN: 0027-8424