Abstract
We have developed a new technique to monitor photophysical relaxation precesses with the resolution inherent in vibrational Raman scattering. We examine the ground-state ultraviolet resonance Raman saturation behavior of tryptophan derivatives. We derive an expression for Raman saturation in a low laser pulse energy flux regime. We demonstrate the utility of the new technique for studying tryptophan and tyrosine excited-state relaxation rates in proteins and for investigating the interaction of dyes with DNA.
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