Raman scattering of some synthetic polypeptides: Poly(γ‐benzyl <scp>L</scp>‐glutamate), poly‐<scp>L</scp>‐leucine, poly‐<scp>L</scp>‐valine, and poly‐<scp>L</scp>‐serine

Abstract

Abstract The Raman spectra of poly‐γ‐benzyl‐ L ‐glutamate, poly‐ L ‐leucine, poly‐ L ‐valine, and poly‐ L ‐serine are reported. For the α‐helical polymers, the conformationally sensitive amide I, II, and III modes are observed in the Raman as, well as the infrared. For the β form, the Raman effect, supplies the infrared inactive inphase motion which is useful for the determination of a parallel or antiparallel chain alignment. Modes characteristic of the specific polypeptide are also observed which are insensitive to conformation.