Anders Irbäck
Professor
Sequence-based study of two related proteins with different folding behaviors
Författare
Summary, in English
Z(SPA-1) is an engineered protein that binds to its parent, the three-helix-bundle Z domain of staphylococcal protein A. Uncomplexed Z(SPA-1) shows a reduced helix content and a melting behavior that is less cooperative, compared with the wild-type Z domain. Here we show that the difference in folding behavior between these two sequences can be partly understood in terms of an off-lattice model with 5-6 atoms per amino acid and a minimalistic potential, in which folding is driven by backbone hydrogen bonding and effective hydrophobic attraction. (C) 2003 Wiley-Liss, Inc.
Avdelning/ar
- Beräkningsbiologi och biologisk fysik - Genomgår omorganisation
Publiceringsår
2004
Språk
Engelska
Sidor
8-12
Publikation/Tidskrift/Serie
Proteins
Volym
54
Issue
1
Dokumenttyp
Artikel i tidskrift
Förlag
John Wiley & Sons Inc.
Ämne
- Biophysics
Nyckelord
- bundle
- Monte Carlo simulation
- folding thermodynamics
- protein folding
- folding kinetics
- three-helix
- unstructured protein
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 0887-3585