A Simple Protein Purification and Folding Experiment for General Chemistry Laboratory

• Robert Bowen ^[1] ; Richard Hartung ^[1] ; Yvonne M. Gindt ^[1]
  1. [1] Department of Chemistry, University of Nebraska
• Localización: Journal of chemical education, ISSN 0021-9584, Vol. 77, Nº 11 (November), 2000, págs. 1456-1456
• Idioma: inglés
• Texto completo no disponible (Saber más ...)
• Resumen

  • 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.