| Two-dimensional infrared (2D IR) spectroscopy has become a useful tool for studying the structure and dynamics of difficult to study biological systems, such as amyloid and membrane proteins. The goals of my research involved measuring the structure of the causative agent in Type 2 diabetes, human amylin, and measuring the structure of the membrane-bound anti-microbial peptide, ovispirin. Human amylin misfolds into beta-sheets, while ovispirin is an alpha-helix on bilayers. In both cases, we exploited vibrational couplings between synthetically incorporated isotope labeled amino acids. Doing so, we achieved site-specific resolution, and when combined with our ability to measure spectra on-the-fly, we were able to monitor previously difficult to observe structural changes in both peptides. |
