An externally funded research project based on the interaction of the heat shock system with electrophilic molecules has been included in a junior/senior biochemistry lab for each of the last three years. Each year, emphasis in the project has changed, beginning with mutation, expression and purification of a heat shock protein (Hsp70) in the first year and shifting more to analysis of the effects of mutation and electrophilic adduction on the protein. At the end of the project, students write a final report on their project and also present their data to the class. The first year of the project resulted in the production of several cysteine to serine mutants of Hsp70, which were then purified by affinity chromatography. Following the nickel-NTA affinity purification, either analysis of chaperone re-folding or binding to co-chaperone protein, Hsp40, was performed. The third year of this project is currently underway. The successes and challenges that have been observed with this project will be discussed, focusing on student interaction with the primary literature, design of experiments by students and overall experimental success.

Bringing a stress-response research project into the biochemistry laboratory

253rd National Meeting (2017)

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