dorsal/arxiv
View SchemaSolvation model dependency of helix-coil transition in polyalanine
| Authors | Y. Peng, U. H. E. Hansmann |
|---|---|
| Categories | |
| ArXiv ID | physics/0202034 |
| URL | https://arxiv.org/abs/physics/0202034 |
| DOI | 10.1016/S0006-3495(02)75668-3 |
| Journal | Biophysical Journal vol. 82 (2002) 3269-3276 |
Abstract
Helix-coil transitions in poly-alanine molecules of length 10 are studied by multicanonical Monte Carlo simulations. The solvation effects are included by either a distance-dependent dielectric permittivity or by a term that is proportional to the solvent-accessible surface area of the peptide. We found a strong dependence of the characteristics of the helix-coil transition from the details of the solvation model.
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"abstract": "Helix-coil transitions in poly-alanine molecules of length 10 are studied by\nmulticanonical Monte Carlo simulations. The solvation effects are included by\neither a distance-dependent dielectric permittivity or by a term that is\nproportional to the solvent-accessible surface area of the peptide. We found a\nstrong dependence of the characteristics of the helix-coil transition from the\ndetails of the solvation model.",
"arxiv_id": "physics/0202034",
"authors": [
"Y. Peng",
"U. H. E. Hansmann"
],
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"physics.bio-ph",
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"doi": "10.1016/S0006-3495(02)75668-3",
"journal_ref": "Biophysical Journal vol. 82 (2002) 3269-3276",
"title": "Solvation model dependency of helix-coil transition in polyalanine",
"url": "https://arxiv.org/abs/physics/0202034"
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