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  Home > JCE Print > Journal of Chemical Education > Issues > 1999  > September  >
In the Laboratory
Determination of Myoglobin Stability by Visible Spectroscopy
Paul A. Sykes, Harn-Cherng Shiue, Jon R. Walker, and Robert C. Bateman Jr.
Department of Chemistry and Biochemistry, The University of Southern Mississippi, Hattiesburg, MS 39406-5043
Cover
September 1999
Vol. 76 No. 9
p. 1283
Abstract
A simple system for the determination of protein stability by denaturation is described. The denaturation of myoglobin by the chaotropic salt guanidium hydrochloride is readily and reproducibly followed at 409 nm, and the free energy of stabilization of the native protein is derived from a straightforward mathematical analysis of the denaturation profile. The use of a well-characterized protein and an inexpensive procedure make this an attractive experiment for general use. Several complementary biophysical experiments are also possible, including the varying of denaturants, temperature, or myoglobin source.
More Information
*  Citation
 Sykes, Paul A.; Shiue, Harn-Cherng; Walker, Jon R.; Bateman, Robert C., Jr. J. Chem. Educ. 1999 76 1283.
*  Keywords
 Biochemistry; Proteins / Peptides; Biophysical Chemistry; Laboratory Instruction
*  History
 Created:
Last Updated:		 July 30, 1999
June 23, 2005
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