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

Giorgio Favrin·Anders Irbäck·Stefan Wallin
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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.

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Giorgio Favrin, Anders Irbäck, Stefan Wallin. 2003-12-30. Sequence-based study of two related proteins with different folding behaviors. https://arxiv.org/abs/q-bio/0312047

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