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  Home > JCE Print > Journal of Chemical Education > Issues > 2000  > November  >
In the Laboratory
A Simple Protein Purification and Folding Experiment for General Chemistry Laboratory
Robert Bowen, Richard Hartung, and Yvonne M. Gindt
Department of Chemistry, University of Nebraska at Kearney, Kearney, NE 68849-1150
Cover
November 2000
Vol. 77 No. 11
p. 1456
Abstract
Most general chemistry laboratories contain a surfeit of inorganic chemistry and little or no biochemistry. We describe a simple procedure for the crude purification of a chromoprotein suitable for a general chemistry laboratory. The protein, phycocyanin, is easy to purify and very stable. It contains a chromophore that can serve to report the integrity of the protein structure: the chromoprotein is dark blue when the protein is folded in its native conformation, and it turns a very pale blue when the protein is unfolded or denatured. The students must identify intermolecular forces present in the co-solvents added and determine their effect on the protein structure. The simplicity of the protein purification procedure will allow phycocyanin to be readily adopted in the general chemistry laboratory.
Supplement
Background information, instructions and handouts for students, and notes for the instructor are available.
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*  Citation
 Bowen, Robert ; Hartung, Richard; Gindt, Yvonne M. J. Chem. Educ. 2000 77 1456.
*  Keywords
 General Chemistry; Intermolecular Forces; Luminescence; Proteins / Peptides; UV-Vis Spectroscopy
*  History
 Created:
Last Updated:		 October 6, 2000
August 31, 2005
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