RUI: Application of Temperature Derivative Spectroscopy to Protein Folding

Texas A&M University Corpus Christi, Corpus Christi TX

Investigators

Abstract

The Experimental Physical Chemistry program and the Biomolecular Systems Cluster support the research of Timothy Causgrove and undergraduate research students at Texas A&M University-Corpus Christi. The goal of this research is develop and use temperature-derivative spectroscopy (TDS) for measuring energy barriers to protein folding. To implement TDS in this project, a light-induced pH jump will be used to initiate folding of the protein at low temperature. The pH jump will cause the protein to fold when the temperature exceeds the energy barrier. Following the pH jump, the temperature will be slowly raised, and the progress of folding vs. temperature will be monitored by infrared absorption spectroscopy. TDS is complementary to kinetic measurements because it directly measures the distribution of energy barriers to protein folding. The initial sample will be polyglutamate, which is well-known to fold as the pH is increased. Causgrove and his students then will apply this technique to short helical peptides and small proteins. Development of the TDS technique is expected to provide an important means of characterizing the energy barriers to protein folding, leading to increased understanding of how a particular protein sequence leads to its biological function. This interdisciplinary research will be carried out with undergraduates at Texas A&M University-Corpus Christi and will provide research experiences for a significant number of Hispanic students. Techniques and results from the research also will be incorporated into undergraduate courses in physical chemistry and physical biochemistry.