The purpose of this research is to develop an experiment that incorporates high-performance liquid chromatography (HPLC) into the biochemistry laboratory curriculum in an innovative way. With this experience, students will utilize HPLC to explore several important biochemistry concepts simultaneously, including intramolecular interactions in protein structure, disulfide bond manipulation, and oxidation-reduction in the protein. Using this method we have investigated a few small monomeric proteins including lysozyme found in chicken egg white, bovine pancreatic trypsin, trypsin inhibitor (aprotinin), and ribonuclease A. The chromatographic method, native storage conditions, denatured conditions, and reduced conditions were optimized for each protein. The retention times of the native, denatured and reduced forms of each protein were analyzed and compared. We hope to incorporate this experiment into the biochemistry laboratory curriculum this coming spring.

Incorporating HPLC into the biochemistry laboratory curriculum in a innovative way

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