Raman optical activity (ROA) is a relatively new method combining the variability of scattering experiments with the structural sensitivity of chiral spectroscopy. Typically, ROA can be employed to determine absolute configuration (AC) of organic compounds, chiral metal complexes, and conformation of biologically relevant chiral molecules in solution. The present review covers the latest theoretical and experimental studies documenting the possibilities and limitations of the technique to probe molecular structure. The quantum-chemical apparatus necessary for spectral interpretation is introduced, and example applications provided, including recent data on possible extensions of the ROA spectroscopy to a more diverse systems. Josef Kapitán received his PhD from the Charles University in Prague in 2006 such as in the eld of Raman optical activity (ROA), with Petr Bouř and Vladimír Baumruk. As a postdoc, he stayed with Laurence D. Barron and Lutz Hecht at the University of Glasgow, simulating Raman optical activity of biopolymers and developing ultraviolet ROA instrument for pre-resonant studies. Since 2010 he is leading a laboratory of Raman spectroscopy at Palacký University in Olomouc. His scientic interest involves instrumentation of optical spectroscopy targeted to elucidation of peptide and protein structure.

The ability to detect chirality gives stereochemically attuned nanosensors the potential to revolutionize the study of biomolecular processes. Such devices may structurally characterize the mechanisms of protein-ligand binding, the intermediates of amyloidogenic diseases and the effects of phosphorylation and glycosylation. We demonstrate that single nanoparticle plasmonic reporters, or nanotags, can enable a stereochemical response to be transmitted from a chiral analyte to an achiral benzotriazole dye molecule in the vicinity of a plasmon resonance from an achiral metallic nanostructure. The transfer of chirality was verified by the measurement of mirror image surface enhanced resonance Raman optical activity spectra for the two enantiomers of both ribose and tryptophan. Computational modelling confirms these observations and reveals the novel chirality transfer mechanism responsible. This is the first report of colloidal metal nanoparticles in the form of single plasmonic substrates displaying an intrinsic chiral sensitivity once attached to a chiral molecule.

Accessible values of the φ and ψ torsional angles determining peptide main chain conformation are traditionally displayed in the form of Ramachandran plots. The number of experimental methods making it possible to determine such conformational distribution is limited. In the present study, Raman optical activity (ROA) spectra of Ac-Ala-NHMe were measured and fit by theoretical curves. This revealed the most favored conformers and a large part of the potential energy surface (PES) of this model dipeptide. Such experimental PES compares well to quantum chemical computations, whereas molecular dynamics (MD) modeling reproduces it less faithfully. The surface shape is consistent with the temperature dependence of the spectra, as observed experimentally and predicted by MD. Despite errors associated with spectral modeling and the measurement, the results are likely to facilitate future applications of ROA spectroscopy.