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  Home > JCE Print > Journal of Chemical Education > Issues > 2000  > March  >
In the Laboratory
Thermal Denaturation of Proteins Studied by UV Spectroscopy
Natasa Poklar and Gorazd Vesnaver
Faculty of Chemistry and Chemical Technology, University of Ljubljana, Askerceva 5, 1000 Ljubljana, Slovenia
Cover
March 2000
Vol. 77 No. 3
p. 380
Abstract
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.
Supplement
Experimental procedures, Data Analysis of the UV-Melting Curves, and a table are included.
*  Contents
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*  Citation
 Poklar, Natasa; Vesnaver, Gorazd. J. Chem. Educ. 2000 77 380.
*  Keywords
 Biophysical Chemistry; UV-Vis Spectroscopy; Undergraduate Research
*  History
 Created:
Last Updated:		 February 14, 2000
August 31, 2005
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