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Circular Dichroism Method for Heat Capacity Determination of Proteins

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Cecil L. Jones , Chris Bailey and Kiran Kumar Bheemarti

Department of Chemistry, University of South Alabama, Mobile, AL 36688-0002

J. Chem. Educ., 2006, 83 (7), p 1067

DOI: 10.1021/ed083p1067

Publication Date (Web): July 1, 2006

Section:

History, Education, and Documentation

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, T_m, occurred with increasing concentration of the strong protein denaturant. van Hoff enthalpy changes, ΔH°, were calculated and plotted as a function of T_m to determine the heat capacity change, ΔC_p, for denaturation. A value of 4.02 ± 0.02 kJ mol^–1 K^–1 was calculated from d( ΔH)/d(ΔT_m). Reported values for ΔC_p range from 4.2 to 9.6 kJ mol^–1 K^–1. The shift in T_m for RNase A with increasing concentration of GuHCl suggests that the protein is undergoing substantial changes in its secondary structure.

Keywords (Audience):

Upper-Division Undergraduate

Keywords (Domain):

Analytical Chemistry

Keywords (Pedagogy):

Hands-On Learning / Manipulatives

Keywords (Subject):

Bioenergetics

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This article has been cited by 1 ACS Journal articles (1 most recent appear below).

Circular Dichroism Spectroscopy in the Undergraduate Curriculum
Adam R. Urbach
Journal of Chemical Education2010 87 (9), 891-893
- Circular Dichroism Spectroscopy in the Undergraduate Curriculum
  Adam R. Urbach
  Journal of Chemical Education2010 87 (9), 891-893
  Circular dichroism spectropolarimetry (CD) is a method of optical spectroscopy that seems in most practical ways like UV−visible spectroscopy. The main difference between the two methods is that CD, instead of measuring the absorbance of light as a ...
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