Resumen de A Full-Semester Biochemistry Laboratory Synchronous with Lecture to Enhance Student Learning and Engagement
Matthew D. Shannon, Jake Simmons
This work outlines a full-semester undergraduate biochemistry laboratory module that is mostly synchronous with the lecture. The pedagogical motivation and design of these experiments are to create a laboratory experience that engages students, prepares students for research, and helps students learn challenging biochemical topics. The laboratory experiment begins with a bioinformatics study of the four proteins used: Horseradish peroxidase (HRP), human serum albumin (HSA), lysozyme, and myoglobin. Initially, HSA and HRP are purified using anion-exchange chromatography and ConA affinity chromatography, respectively, from a solution of the four proteins. The purification of each protein is then estimated by SDS-PAGE gel electrophoresis and quantified by UV–vis spectroscopy. Following the purification of HSA, a 1H NMR ligand binding experiment is conducted. Following the purification of HRP, a UV–vis kinetics experiment is conducted with and without an inhibitor and analyzed using Michaelis–Menten kinetics. Upon successful completion of all the experiments, groups give 20 min presentations to summarize their results. This experiment has been completed by 12 groups over two semesters at a small primarily undergraduate institution (PUI) with promising assessment data and positive feedback. Approximately 75% of students retained their conceptual understanding of biochemical topics throughout the semester, and students overwhelmingly highlighted the importance that the experiments were related to the lecture and built on each other each week.
