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

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dc.creatorFavrin, Giorgio
dc.creatorIrbäck, Anders
dc.creatorWallin, Stefan
dc.date2003-12-30
dc.date.accessioned2026-07-07T05:58:05Z
dc.date.available2026-07-07T05:58:05Z
dc.descriptionZSPA-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.
dc.description12 pages, 5 figures
dc.identifierhttps://arxiv.org/abs/q-bio/0312047
dc.identifierhttp://arxiv.org/abs/q-bio/0312047
dc.identifierProteins 54 (2004) 8-12
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/88231
dc.subjectBiomolecules
dc.subjectSoft Condensed Matter
dc.titleSequence-based study of two related proteins with different folding behaviors
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