Sequence-based study of two related proteins with different folding behaviors
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Updated: Aug 29, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
Giorgio Favrin1, Anders Irbäck, Stefan Wallin
1Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden.
Abstract:
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.
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