X-ray Crystallography of -Peptide Foldamers

X-ray Crystallography of -Peptide Foldamers

This research project explores theoretical and practical aspects of X-ray crystallography in the context of an ongoing international collaboration with the Pohang Accelerator Laboratory. By utilizing symmetry elements and computational techniques of X-ray crystallography, I am attempting to determine the solid- state structure of a -amino acid oligomer foldamer from an incomplete data set. The goal of this research project is to obtain an accurate and precise final structure for this amino acid foldamer. Through elaborate computational analysis, a preliminary single crystal X-ray diffraction structure has been solved as isopropylNH-(ACPC-Aib)3-OBn and is currently under crystallographic refinement. Once future refinement has been completed, the three-dimensional crystallographic structure and intramolecular forces of the final structure will be obtained and further analyzed, including but not limited to observing the self- assembling properties of this organic material.