Creating an Exploratory Protocol of Protein Thermodynamics for Chemistry Undergraduates

Kryzsko Commons Ballroom, Winona, Minnesota

The objective of this research is to create a protocol that explores the protein unfolding process and its thermodynamic properties using circular dichroism (CD) spectroscopy and differential scanning fluorimetry (DSF) for chemistry undergraduates. The thermodynamic properties of interest for the unfolding process are the standard enthalpy change (ΔH°), the standard entropy changes (ΔS°), the equilibrium constant (K) and melting temperature (Tm). The CD instrument explores these thermodynamic properties by utilizing the thermal denaturation scan (TD scan). Alongside the TD scan, the CD instrument can also explore the makeup of the protein using the wavelength scan (WL scan). The WL scan is able to provide information on the secondary structure of the protein. These results can provide an understanding when exploring the thermodynamic properties of a protein. With the creation of this protocol, it was decided that the students are required design an overall research question with a testable hypothesis. The protocol provided underwent a test run with chemistry students and feedback was obtained. The results of this research found that the protocol for undergraduate chemistry majors provided a well developed understanding of protein thermodynamics and structure.