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Polymer Principles of Protein Calorimetric Two-State Cooperativity | Huseyin Kaya
; Hue Sun Chan
; | Date: |
29 Mar 2000 | Journal: | Proteins: Struc. Func. & Gen., 40 (2000) 637 | Subject: | Statistical Mechanics; Soft Condensed Matter | cond-mat.stat-mech cond-mat.soft q-bio | Abstract: | The experimental calorimetric two-state criterion requires the van’t Hoff enthalpy $Delta H_{
m vH}$ around the folding/unfolding transition midpoint to be equal or very close to the calorimetric enthalpy $Delta H_{
m cal}$ 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 $Delta H_{
m vH}$’s being approximately equal to $Delta H_{
m cal}$ 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’’ $T_{
m f}/T_{
m g}$ 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. | Source: | arXiv, cond-mat/0003479 | Services: | Forum | Review | PDF | Favorites |
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