
Anders Irbäck
Professor

Sequence-based study of two related proteins with different folding behaviors
Author
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.
Department/s
- Computational Biology and Biological Physics - Undergoing reorganization
Publishing year
2004
Language
English
Pages
8-12
Publication/Series
Proteins
Volume
54
Issue
1
Document type
Journal article
Publisher
John Wiley & Sons Inc.
Topic
- Biophysics
Keywords
- bundle
- Monte Carlo simulation
- folding thermodynamics
- protein folding
- folding kinetics
- three-helix
- unstructured protein
Status
Published
ISBN/ISSN/Other
- ISSN: 0887-3585