Thermal Denaturation of Proteins Studied by UV Spectroscopy
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Natasa Poklar [1] ; Gorazd Vesnaver [1]
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[1] University of Ljubljana
University of Ljubljana
Eslovenia
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- Localización: Journal of chemical education, ISSN 0021-9584, Vol. 77, Nº 3 (March), 2000, págs. 380-380
- Idioma: inglés
- Texto completo no disponible (Saber más ...)
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Resumen
UV spectroscopy has been widely used for monitoring the unfolding of proteins. During temperature-induced denaturation the protein absorbance changes with temperature until the process of unfolding is completed. Analysis of the measured absorbance-vs-temperature curve (UV melting curve) based on the two-state approximation of the denaturation process leads to the van't Hoff enthalpy of denaturation at the temperature of the half-transition, DH°(Td), and the corresponding entropy of denaturation, DS°(Td). A determination of DH°(Td) and DS°(Td) for a-chymotrypsinogen A at pH 3.0 from the experimental UV melting curve is demonstrated.
