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Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

Hydrogen bonds, hydrophobicity forces and the character of the collapse transition

Author

  • A Irbäck
  • F Sjunnesson
  • S Wallin

Summary, in English

We study the thermodynamic behavior of a model protein with 54 amino acidsthat is designed to form 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 torsion angles as its only degrees of freedom.The force field is based on hydrogen bonds and effective hydrophobicity forces. We study how the character of the collapse transition depends on the strengths of these forces. For a suitable choice of these two parameters, it is found that the collapse transition is first-order-like and coincides with the folding transition. Also shown is that the corresponding one- and two-helix segments make less stable secondary structure than the three-helix sequence.

Department/s

  • Computational Biology and Biological Physics

Publishing year

2001-06

Language

English

Pages

79-169

Publication/Series

Journal of Biological Physics

Volume

27

Issue

2-3

Document type

Journal article

Publisher

Kluwer

Status

Published

ISBN/ISSN/Other

  • ISSN: 0092-0606