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Foto på Anders Irbäck

Anders Irbäck

Professor

Foto på Anders Irbäck

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

Författare

  • 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.

Avdelning/ar

  • Beräkningsbiologi och biologisk fysik - Har omorganiserats

Publiceringsår

2001-06

Språk

Engelska

Sidor

79-169

Publikation/Tidskrift/Serie

Journal of Biological Physics

Volym

27

Issue

2-3

Dokumenttyp

Artikel i tidskrift

Förlag

Springer

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0092-0606