dorsal/arxiv
View SchemaSequence-based study of two related proteins with different folding behaviors
| Authors | Giorgio Favrin, Anders Irbäck, Stefan Wallin |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0312047 |
| URL | https://arxiv.org/abs/q-bio/0312047 |
| Journal | Proteins 54 (2004) 8-12 |
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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"abstract": "ZSPA-1 is an engineered protein that binds to its parent, the\nthree-helix-bundle Z domain of staphylococcal protein A. Uncomplexed ZSPA-1\nshows a reduced helix content and a melting behavior that is less cooperative,\ncompared with the wild-type Z domain. Here we show that the difference in\nfolding behavior between these two sequences can be partly understood in terms\nof an off-lattice model with 5-6 atoms per amino acid and a minimalistic\npotential, in which folding is driven by backbone hydrogen bonding and\neffective hydrophobic attraction.",
"arxiv_id": "q-bio/0312047",
"authors": [
"Giorgio Favrin",
"Anders Irb\u00e4ck",
"Stefan Wallin"
],
"categories": [
"q-bio.BM",
"cond-mat.soft"
],
"journal_ref": "Proteins 54 (2004) 8-12",
"title": "Sequence-based study of two related proteins with different folding behaviors",
"url": "https://arxiv.org/abs/q-bio/0312047"
},
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"execution_id": "856352db-a657-48e0-9557-4e259e3ac798",
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"variant": "snapshot-2026-03-01",
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