Premium
Raman scattering of some synthetic polypeptides: Poly(γ‐benzyl L ‐glutamate), poly‐ L ‐leucine, poly‐ L ‐valine, and poly‐ L ‐serine
Author(s) -
Koenig J. L.,
Sutton P. L.
Publication year - 1971
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360100108
Subject(s) - chemistry , antiparallel (mathematics) , valine , raman spectroscopy , serine , amide , monomer , leucine , polymer , stereochemistry , amino acid , biochemistry , organic chemistry , physics , quantum mechanics , magnetic field , optics , enzyme
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.