Theoretical simulation of the ROA spectra of neutral cysteine and serine

Vibrational Raman Optical Activity (ROA) spectra have been calculated for neutral conformations of amino acids cysteine and serine. The purpose of the study was to investigate the conformational dependence of the ROA differential intensity, paying particular attention to the conformation of the polar side chains. In cysteine, the ROA intensities of side chain vibrations tend to vary fairly regularly with the value of the θ(NCCS) dihedral angle, while for serine the formation of hydrogen bonds by the side chain hydroxyl group seems to be the deciding factor determining the ROA intensities of the side chain vibrations.