A Simple Protein Purification and Folding Experiment for General Chemistry Laboratory
Document Type
Article
Publication Date
11-1-2000
Journal / Book Title
Journal of Chemical Education
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.
DOI
10.1021/ed077p1456
Montclair State University Digital Commons Citation
Bowen, Robert; Hartung, Richard; and Gindt, Yvonne, "A Simple Protein Purification and Folding Experiment for General Chemistry Laboratory" (2000). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 545.
https://digitalcommons.montclair.edu/chem-biochem-facpubs/545