dorsal/arxiv
View SchemaFolding thermodynamics of peptides
| Authors | Anders Irbäck, Sandipan Mohanty |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0412007 |
| URL | https://arxiv.org/abs/q-bio/0412007 |
| DOI | 10.1529/biophysj.104.050427 |
| Journal | Biophys. J. 88 (2005) 1560-1569 |
Abstract
A simplified interaction potential for protein folding studies at the atomic level is discussed and tested on a set of peptides with about 20 residues each. The test set contains both alpha-helical (Trp cage, Fs) and beta-sheet (GB1p, GB1m2, GB1m3, Betanova, LLM) peptides. The model, which is entirely sequence-based, is able to fold these different peptides for one and the same choice of model parameters. Furthermore, the melting behavior of the peptides is in good quantitative agreement with experimental data. Apparent folded populations obtained using different observables are compared, and are found to be very different for some of the peptides (e.g., Betanova). In other cases (in particular, GB1m2 and GB1m3), the different estimates agree reasonably well, indicating a more two-state-like melting behavior.
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"abstract": "A simplified interaction potential for protein folding studies at the atomic\nlevel is discussed and tested on a set of peptides with about 20 residues each.\nThe test set contains both alpha-helical (Trp cage, Fs) and beta-sheet (GB1p,\nGB1m2, GB1m3, Betanova, LLM) peptides. The model, which is entirely\nsequence-based, is able to fold these different peptides for one and the same\nchoice of model parameters. Furthermore, the melting behavior of the peptides\nis in good quantitative agreement with experimental data. Apparent folded\npopulations obtained using different observables are compared, and are found to\nbe very different for some of the peptides (e.g., Betanova). In other cases (in\nparticular, GB1m2 and GB1m3), the different estimates agree reasonably well,\nindicating a more two-state-like melting behavior.",
"arxiv_id": "q-bio/0412007",
"authors": [
"Anders Irb\u00e4ck",
"Sandipan Mohanty"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1529/biophysj.104.050427",
"journal_ref": "Biophys. J. 88 (2005) 1560-1569",
"title": "Folding thermodynamics of peptides",
"url": "https://arxiv.org/abs/q-bio/0412007"
},
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