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Giorgio Favrin, Anders Irbäck and Stefan
Wallin
Sequence-Based Study of Two Related Proteins with
Different Folding Behaviors
Proteins: Structure, Function, and Bioinformatics
54, 8-12 (2004)
Abstract
ZSPA-1 is an engineered protein
that binds to its parent, the three-helix-bundle Z domain
of staphylococcal protein A. Uncomplexed ZSPA-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.
LU TP 03-14
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