Anders Irbäck
Professor
Three-helix-bundle protein in a Ramachandran model
Författare
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.
Avdelning/ar
- Beräkningsbiologi och biologisk fysik - Genomgår omorganisation
Publiceringsår
2000-12-05
Språk
Engelska
Sidor
8-13614
Publikation/Tidskrift/Serie
Proceedings of the National Academy of Sciences
Volym
97
Issue
25
Dokumenttyp
Artikel i tidskrift
Förlag
National Academy of Sciences
Nyckelord
- Models, Molecular
- Protein Conformation
- Proteins
- Thermodynamics
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 0027-8424