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Foto på Anders Irbäck

Anders Irbäck

Professor

Foto på Anders Irbäck

A minimalistic all-atom approach to protein folding

Författare

  • Anders Irbäck

Summary, in English

Using simple sequence-based potentials, the folding properties of a designed three-helix-bundle protein, an alpha-helix and a beta-hairpin are studied. The three-helix-bundle protein is modelled using 5-6 atoms per amino acid and is found to undergo a first-order-like folding transition in which chain collapse and helix formation cannot be separated, which is in-accord with experimental data. The other two sequences are studied using a model that contains all atoms and are indeed found to make an alpha-helix and a beta-hairpin, respectively, for exactly the same choice of parameters. The calculated melting curves are, moreover, in reasonable quantitative agreement with experimental data, for both peptides. The melting curves are found to be quite well described by a simple two-state model, although the energy distributions lack a clear bimodal shape.

Avdelning/ar

  • Beräkningsbiologi och biologisk fysik - Genomgår omorganisation

Publiceringsår

2003

Språk

Engelska

Sidor

1797-1807

Publikation/Tidskrift/Serie

Journal of Physics: Condensed Matter

Volym

15

Issue

18

Dokumenttyp

Artikel i tidskrift

Förlag

IOP Publishing

Ämne

  • Biophysics

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1361-648X