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Far‐infrared spectra of sequential polypeptides with α‐helical and polyglycine II structures
Author(s) -
Itoh Koichi,
Katabuchi Hiroaki
Publication year - 1973
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.1973.360120419
Subject(s) - chemistry , alanine , valine , infrared spectroscopy , phenylalanine , glycine , amino acid , crystallography , infrared , leucine , monomer , proline , spectral line , stereochemistry , amino acid residue , peptide sequence , organic chemistry , polymer , biochemistry , physics , astronomy , optics , gene
The sequential copolymers of glycine and L ‐alanine, L‐valine and L ‐alanine, L‐leucine and L ‐alanine, and L‐phenylalanine and L ‐alanine and those containing the L‐proline residues were synthesized. The infrared spectra in the region from 700 to 200 cm ‐1 were measured for these polypeptides with the α‐helical conformation or the polyglycine II structure and compared with the spectra of the β‐form structures. The results showed that several infrared bands observed in the region from 600 to 200 cm ‐1 clearly reflect not only the backbone conformations but also the local conformations of component amino acid residues of polypeptides with the α‐helical, β‐form and polyglycine II structures.