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Heat of denaturation of lysozyme
Author(s) -
O'Reilly J. M.,
Karasz F. E.
Publication year - 1970
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1970.360091205
Subject(s) - chemistry , lysozyme , enthalpy , denaturation (fissile materials) , thermodynamics , aqueous solution , heat capacity , mole , organic chemistry , biochemistry , nuclear chemistry , physics
The enthalpy of denaturation of lysozyme was determined by measuring the heat, capacity of an aqueous solution of this protein in the vicinity of the transition temperature, 46 °C at pH 1. Within experimental error the calorimetric, heat (56 ± 8 kcal/mole) was found to agree with the van't Hoff transition enthalpy (63 ± 6 kcal/mole) determined from optical rotation measurements as a function of temperature. This indicates that denaturation of this protein can be interpreted in terms of a two‐state model. Successive measurements of the same sample showed, from several lines of evidence, that the transition was about 80% reversible for the particular environmental conditions and thermal history involved in the study.