Infrared Spectroscopy of Amino Acid Side Chains

Abstract

Infrared structural biology is a novel and promising approach for detecting structure and functional processes of proteins. However, the process of assignment of infrared signals to specific amino acid side chains in a protein requires further development. For our experiment, we examined individual amino acids to help understand how they contribute to infrared signals of intact proteins. Specifically, we worked with arginine, histidine, and lysine. The long-term goal of this experiment is to create a definitive map of the FTIR spectra for each of these amino acids. We measured the infrared absorbance of these three amino acid side chains. Measuring and comparing the results of the different amino acids and different volume sizes allowed us to define optimal experimental conditions for these measurements.