dorsal/arxiv
View SchemaFinite size effects on thermal denaturation of globular proteins
| Authors | Mai Suan Li, D. K. Klimov, D. Thirumalai |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0411050 |
| URL | https://arxiv.org/abs/q-bio/0411050 |
| DOI | 10.1103/PhysRevLett.93.268107 |
Abstract
Finite size effects on the cooperative thermal denaturation of proteins are considered. A dimensionless measure of cooperativity, Omega, scales as N^zeta, where N is the number of amino acids. Surprisingly, we find that zeta is universal with zeta = 1 + gamma, where the exponent gamma characterizes the divergence of the susceptibility for a self-avoiding walk. Our lattice model simulations and experimental data are consistent with the theory. Our finding rationalizes the marginal stability of proteins and substantiates the earlier predictions that the efficient folding of two-state proteins requires the folding transition temperature to be close to the collapse temperature.
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"abstract": "Finite size effects on the cooperative thermal denaturation of proteins are\nconsidered. A dimensionless measure of cooperativity, Omega, scales as N^zeta,\nwhere N is the number of amino acids. Surprisingly, we find that zeta is\nuniversal with zeta = 1 + gamma, where the exponent gamma characterizes the\ndivergence of the susceptibility for a self-avoiding walk. Our lattice model\nsimulations and experimental data are consistent with the theory. Our finding\nrationalizes the marginal stability of proteins and substantiates the earlier\npredictions that the efficient folding of two-state proteins requires the\nfolding transition temperature to be close to the collapse temperature.",
"arxiv_id": "q-bio/0411050",
"authors": [
"Mai Suan Li",
"D. K. Klimov",
"D. Thirumalai"
],
"categories": [
"q-bio.BM",
"q-bio.QM"
],
"doi": "10.1103/PhysRevLett.93.268107",
"title": "Finite size effects on thermal denaturation of globular proteins",
"url": "https://arxiv.org/abs/q-bio/0411050"
},
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