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Far-infrared spectra of sequential polypeptides with α-helical and polyglycine II structures

✍ Scribed by Koichi Itoh; Hiroaki Katabuchi

Publisher
Wiley (John Wiley & Sons)
Year
1973
Tongue
English
Weight
452 KB
Volume
12
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

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.

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