Resumen de A Simple Protein Purification and Folding Experiment for General Chemistry Laboratory
Robert Lowen, Richard Hartung, Yvonne M. Gindt
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.
