dorsal/arxiv
View SchemaFinite size effects on calorimetric cooperativity of two-state proteins
| Authors | Mai Suan Li, D. K. Klimov, D. Thirumalai |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0412008 |
| URL | https://arxiv.org/abs/q-bio/0412008 |
| DOI | 10.1016/j.physa.2004.11.029 |
Abstract
Finite size effects on the calorimetric cooperatity of the folding-unfolding transition in two-state proteins are considered using the Go lattice models with and without side chains. We show that for models without side chains a dimensionless measure of calorimetric cooperativity kappa2 defined as the ratio of the van't Hoff to calorimetric enthalpy does not depend on the number of amino acids N. The average value of kappa2 is about 3/4 which is lower than the experimental value kappa2=1. For models with side chains kappa2 approaches unity as kappa2 \sim N^mu, where exponent mu=0.17. Above the critical chain length Nc =135 these models can mimic the truly all-or-non folding-unfolding transition.
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"abstract": "Finite size effects on the calorimetric cooperatity of the folding-unfolding\ntransition in two-state proteins are considered using the Go lattice models\nwith and without side chains. We show that for models without side chains a\ndimensionless measure of calorimetric cooperativity kappa2 defined as the ratio\nof the van\u0027t Hoff to calorimetric enthalpy does not depend on the number of\namino acids N. The average value of kappa2 is about 3/4 which is lower than the\nexperimental value kappa2=1. For models with side chains kappa2 approaches\nunity as kappa2 \\sim N^mu, where exponent mu=0.17. Above the critical chain\nlength Nc =135 these models can mimic the truly all-or-non folding-unfolding\ntransition.",
"arxiv_id": "q-bio/0412008",
"authors": [
"Mai Suan Li",
"D. K. Klimov",
"D. Thirumalai"
],
"categories": [
"q-bio.BM",
"q-bio.QM"
],
"doi": "10.1016/j.physa.2004.11.029",
"title": "Finite size effects on calorimetric cooperativity of two-state proteins",
"url": "https://arxiv.org/abs/q-bio/0412008"
},
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