Finite size effects on calorimetric cooperativity of two-state proteins

Details Finite size effects on calorimetric cooperativity of two-state proteins Finite size effects on calorimetric cooperativity of two-state proteins

2004-12-05

arxiv.org/abs/q-bio/0412008v1

Biology

Quantitative Biology

Biomolecules

3 eps figures. To appear in the special issue of Physica A

Scientific paper

10.1016/j.physa.2004.11.029

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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