Heat of denaturation of lysozyme

✍ Scribed by J. M. O'Reilly; F. E. Karasz

• Book ID: 101717171
• Publisher: Wiley (John Wiley & Sons)
• Year: 1970
• Tongue: English
• Weight: 401 KB
• Volume: 9
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1970.360091205

✦ Synopsis

Abstract

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.