Abstract
The advent of high-power-pulsed lasers, whose wavelength is easily shifted via nonlinear optical techniques (crystal mixers, stimulated Raman shifters) has made possible the routine acquisition of Raman spectra with excitation throughout the UV region. This development has opened the way to systematic exploration of the resonance Raman characteristics of UV chromophores, including the aromatic side chains of proteins as well as the amide bonds of the polypeptide backbone. We analyzed the Raman spectra of these chromophores obtained with 266-, 240-, 218-, and 200-nm excitation from a H2 Raman-shifted Nd:YAG laser.
© 1986 Optical Society of America
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