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  Home > JCE Print > Journal of Chemical Education > Issues > 2006  > July  >
In the Laboratory
Circular Dichroism Method for Heat Capacity Determination of Proteins
Cecil L. Jones, Chris Bailey, and Kiran Kumar Bheemarti
Department of Chemistry, University of South Alabama, Mobile, AL 36688-0002
Cover
July 2006
Vol. 83 No. 7
p. 1067
Abstract
Circular dichroism spectroscopy was used to measure the thermal unfolding of bovine pancreatic ribonuclease A (RNase A) with various concentrations of guanidine hydrochloride (GuHCl). A red shift in transition midpoint temperatures, Tm, occurred with increasing concentration of the strong protein denaturant. van Hoff enthalpy changes, ΔH°, were calculated and plotted as a function of Tm to determine the heat capacity change, ΔCp, for denaturation. A value of 4.02 ± 0.02 kJ mol–1 K–1 was calculated from d( ΔH)/d(ΔTm). Reported values for ΔCp range from 4.2 to 9.6 kJ mol–1 K–1. The shift in Tm for RNase A with increasing concentration of GuHCl suggests that the protein is undergoing substantial changes in its secondary structure.
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*  Citation
 Jones, Cecil L.; Bailey, Chris; Bheemarti, Kiran Kumar. J. Chem. Educ. 2006 83 1067.
*  Keywords
 Analytical Chemistry; Bioanalytical Chemistry; Biochemistry; Bioenergetics; Biophysical Chemistry; Hands-On Learning / Manipulatives; Heat Capacity; Laboratory Instruction; Proteins / Peptides; Spectroscopy; Thermodynamics; Undergraduate Research; Upper-Division Undergraduate
*  History
 Created:
Last Updated:		 5/26/2006
5/31/2006
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