Comparison of Raman scattering spectra for different samples of protium and deuterium water has been done. Registration of spectra was held with the help of fiber optics technique and BWS465-785H small sized spectrometer. For excitation of spontaneous Raman scattering spectra the continuously working laser (λ=785 nm) has been used. The essential differences of low frequency Raman scattering spectra for different water samples have been observed. Such differences have been explained by the presence of structural defects and imperfections in analyzed water. Stimulated Raman scattering spectra in protium and deuterium water have been observed with excitation by picosecond laser pulses with wavelength 532 nm. Low frequency Raman satellites in Stimulated Raman scattering spectra have been recorded, related to clusters of several water molecules.
Raman spectra of tryptophan and tyrosine polycrystals have been analyzed in a wide spectral range by fiber-optic spectroscopy. The Raman spectra have been recorded with a BWS465-785H spectrometer in the spectral range of 0–2700 cm^–1 using a 785-nm cw laser as an excitation source. Parameters of the Raman spectra are compared for three crystalline phase modifications of aromatic amino acids: left-handed, right-handed, and racemic phase. The presence of strong Raman satellites, the characteristics of which change depending on the type of the chiral phase state of amino acid, is found in the low-frequency Raman spectra of tryptophan and tyrosine amino acid lattices. The results obtained can be used for monitoring the chiral purity of bioactive preparations containing amino acids.
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