One project involves measuring the rate of left- to right- handed helical interconversions in peptides of different lengths and in different solvents.  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.

A second project involves the characterization of rates of conformational interconversions of acetylated 7-aminocoumarins.  We are using proton and fluorine NMR spectroscopy to characterize the conformations and the rates of interconversion.

At left is a cartoon of a future project, where the red "ball" at the bottom is an oxygen atom of a serine side chain.  It has been postulated that serine (and other) side chains can hydrogen bond with backbone amide hydrogens, thereby stabilizing helical structures in peptides and proteins.  We plan to measure this stabilization using model peptides and NMR spectroscopy.

Click here for a movie of left- to right-handed helical interconversion!