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

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

2003-12-30

arxiv.org/abs/q-bio/0312047v1

Proteins 54 (2004) 8-12

Biology

Quantitative Biology

Biomolecules

12 pages, 5 figures

Scientific paper

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.

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