dorsal/arxiv
View SchemaStudy of a model for the folding of a small protein
| Authors | Andrea Nobile, Federico Rapuano |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0503034 |
| URL | https://arxiv.org/abs/q-bio/0503034 |
| DOI | 10.1088/0953-8984/18/24/009 |
Abstract
We describe the results obtained from an improved model for protein folding. We find that a good agreement with the native structure of a 46 residue long, five-letter protein segment is obtained by carefully tuning the parameters of the self-avoiding energy. In particular we find an improved free-energy profile. We also compare the efficiency of the multidimensional replica exchange method with the widely used parallel tempering.
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"abstract": "We describe the results obtained from an improved model for protein folding.\nWe find that a good agreement with the native structure of a 46 residue long,\nfive-letter protein segment is obtained by carefully tuning the parameters of\nthe self-avoiding energy. In particular we find an improved free-energy\nprofile. We also compare the efficiency of the multidimensional replica\nexchange method with the widely used parallel tempering.",
"arxiv_id": "q-bio/0503034",
"authors": [
"Andrea Nobile",
"Federico Rapuano"
],
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"q-bio.BM"
],
"doi": "10.1088/0953-8984/18/24/009",
"title": "Study of a model for the folding of a small protein",
"url": "https://arxiv.org/abs/q-bio/0503034"
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