Biophysical Chemistry - The main objectives of the research studies being performed in Dr. Hibbard’s lab have been: (1) to observe alterations in the configuration of the ocular lens structural proteins, alpha- and beta-crystallin, due to the presence of electrolytes, and (2) to determine the extent to which these aqueous crystallin solutions are affected by exposure to near-UV radiation. Since changes in protein structure are proposed to occur concurrently with changes in the spectral properties of tryptophan (Trp) residues within the protein, several spectroscopic techniques are being used to monitor alterations in the structure and microenvironment of Trp residues in these crystallins. Spectral measurements are monitored for samples undergoing timed exposure to 295nm radiation from a 450W xenon lamp under varying NaCl and CaCl2 concentrations. Alpha-crystallin is believed to function as a chaperone to protect structural proteins, such as beta-crystallin, from aggregating in the ocular lens upon being damaged. Turbidity studies are thus performed to analyze effects on the chaperone activity of alpha-crystallin in the presence of heat-aggregated beta-crystallin.
Experimental Techniques – UV-Visible absorbance spectroscopy; steady-state fluorescence spectroscopy; circular dichroism (CD) spectropolarimetry.
Chemical education - Research involving the use of process oriented guided inquiry learning (POGIL) techniques, subject mastery strategies, electronic portfolios, and personal response systems in the curriculum is being performed to determine the effects on student learning and retention of basic chemical knowledge.
