Abstract
Abstract The UV Raman excitation profiles of l‐cystine have been measured between 220 and 514.5 nm. No enhancement is observed from the lowest energy electronic transition (λmax = 245 nm). The excitation profiles for the SS, CS and CO stretching vibrations are each satisfactorily modeled by standard Albrecht A‐term pre‐resonance expressions which indicate that the Raman intensities derive from a state(s) at ca 170 nm which is probably σ → σ* in character. Selective enhancement of disulfide stretching vibrations in proteins will require excitation in the vacuum UV spectral region.
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