Sequence-based study of two related proteins with different folding behaviors.
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.
Favrin
Giorgio
G
Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden.
Irbäck
Anders
A
Wallin
Stefan
S
D000595:Amino Acid Sequence; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009010:Monte Carlo Method; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D020539:Sequence Analysis, Protein / Q000379:methods*; D013205:Staphylococcal Protein A / Q000737:chemistry / Q000235:genetics; D013816:Thermodynamics
D013205:Staphylococcal Protein A