Sequence-based study of two related proteins with different folding behaviors

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.

• Author: Giorgio Favrin; Anders Irbäck; Stefan Wallin
• Department/s: Computational Biology and Biological Physics - Has been reorganised
• Publishing year: 2004
• Language: English
• Pages: 8-12
• Publication/Series: Proteins
• Volume: 54
• Issue: 1
• Links: http://dx.doi.org/10.1002/prot.10575
• 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