Research Interests

My research students and I use infrared and NMR spectroscopies to characterize short helical peptide systems. We use these spectroscopies to measure the natural motions of these molecules, which are short models of larger protein systems. We seek to gain insight into ways helical secondary structures can behave and be monitored in larger protein systems. Our infrared studies employ 310-helical peptides to investigate the peptide and protein Amide I band. Here at Fairfield, we employ “isotope-edited” spectrosocpy to dissect this conformationally diagnostic spectroscopic feature. In collaboration with Professor Timothy Zwier of Purdue University, we examine the gas-phase spectra of short molecules. A second project involves measuring the rate of left- to right- handed helical interconversions of our peptides. By examining peptides of different lengths in a variety of solvents (varying viscosity and H-bonding capacity), we aim to characterize the transition state for the left/right reaction and test fundamental theories of reaction dynamics in the condensed phase.
““Everything that is living can be understood in terms of the jiggling and wiggling of atoms.” --Richard Feynman”