Polymer Principles of Protein Calorimetric Two-State Cooperativity

Details Polymer Principles of Protein Calorimetric Two-State Cooperativity Polymer Principles of Protein Calorimetric Two-State Cooperativity

2000-03-29

arxiv.org/abs/cond-mat/0003479v3

Proteins: Struc. Func. & Gen., 40 (2000) 637

Physics

Condensed Matter

Statistical Mechanics

27 pages, 15 postscripts figures. Accepted for publication in Proteins: Struct. Funct. Genet

Scientific paper

The experimental calorimetric two-state criterion requires the van't Hoff enthalpy $\Delta H_{\rm vH}$ around the folding/unfolding transition midpoint to be equal or very close to the calorimetric enthalpy $\Delta H_{\rm cal}$ of the entire transition. We use an analytical model with experimental parameters from chymotrypsin inhibitor 2 to elucidate the relationship among several different van't Hoff enthalpies used in calorimetric analyses. Under reasonable assumptions, the implications of these $\Delta H_{\rm vH}$'s being approximately equal to $\Delta H_{\rm cal}$ are equivalent: Enthalpic variations among denatured conformations in real proteins are much narrower than some previous lattice-model estimates, suggesting that the energy landscape theory ``folding to glass transition temperature ratio'' $T_{\rm f}/T_{\rm g}$ may exceed 6.0 for real calorimetrically two-state proteins. Several popular three-dimensional lattice protein models, with different numbers of residue types in their alphabets, are found to fall short of the high experimental standard for being calorimetrically two-state. Some models postulate a multiple-conformation native state with substantial pre-denaturational energetic fluctuations well below the unfolding transition temperature and/or predict a significant post-denaturational continuous conformational expansion of the denatured ensemble at temperatures well above the transition point.

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