Resonance Raman spectroscopy

[4] Resonance Raman spectroscopy has been used in the characterization of inorganic compounds and complexes,[5] proteins,[6][7] nucleic acids,[8] pigments,[8] and in archaeology and art history.

[5] Like ordinary Raman spectroscopy, RRS observes vibrational transitions producing a nonzero change in the polarizability of the molecule or material being studied.

[8] By using multiple lasers, pulsed lasers, and/or certain sample preparation techniques, a range of more sophisticated variants of RRS can be performed, including: Because of its selectivity and sensitivity, resonance Raman spectroscopy is typically used to study molecular vibrations in compounds that would have very weak and/or complex Raman spectra in the absence of resonance enhancement.

[8] Dyes and pigments, all of which exhibit electronic transitions in the visible part of the electromagnetic spectrum, were among the first substances to be studied by resonance Raman spectroscopy.

[19] The resonance Raman spectra of other polyene pigments, such as spheroidene and retinal, have been used to identify differences in chromophore conformation in photoactive proteins.

Protein-bound cofactors that absorb in the visible wavelength range, such as heme, flavins, or transition metal complexes, can be examined by RRS with minimal spectral overlap from the rest of the molecule.

Protein folding and denaturation have been examined using deep-UV resonance Raman spectroscopy of the polypeptide backbone, with excitation wavelengths shorter than 200 nm.

[25] Resonance Raman spectroscopy with ultraviolet excitation can be used to examine the chemistry, structure, and intermolecular interactions of nucleic acids, specifically the bases.

[8] Nanowires of inorganic semiconductor materials including gallium phosphide and carbon-encapsulated mercury telluride have also been shown to exhibit resonance Raman spectra with visible excitation light.