
Anders Irbäck
Professor

Three-helix-bundle protein in a Ramachandran model
Author
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 - Undergoing reorganization
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 Academy of Sciences
Keywords
- Models, Molecular
- Protein Conformation
- Proteins
- Thermodynamics
Status
Published
ISBN/ISSN/Other
- ISSN: 0027-8424