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Far‐infrared spectra of poly(‐α‐amino acids) with basic alkyl group side chains
Author(s) -
Itoh Koichi,
Shimanouchi Takehiko,
Oya Masanao
Publication year - 1969
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.1969.360070503
Subject(s) - norvaline , norleucine , chemistry , side chain , valine , alkyl , crystallography , infrared spectroscopy , amino acid , stereochemistry , helix (gastropod) , leucine , organic chemistry , polymer , ecology , biochemistry , snail , biology
Far‐infrared spectra in the region from 700 to 60 cm −1 have been measured for the α‐helix structures of poly( L ‐α‐amino‐ n ‐butyric acid), poly‐ L ‐norvaline, poly‐ L ‐norleucine, and poly‐ L ‐leucine and for the β‐form structures of poly( L ‐α‐amino‐ n ‐butyric acid), poly‐ L ‐valine, poly( DL ‐amino‐ n ‐butyric acid), poly‐ DL ‐norvaline, and poly‐ DL ‐norleucine. The changes of the spectra on N ‐deuteration have been measured in the region between 700 and 400 cm −1 . It is concluded that, the α‐helix has characteristic bauds near 690, 650, 610, 380, 150, and 100 cm −1 , and that the β‐form has characteristic bands near 700, 240, and 120 cm −1 . The main‐chain vibrations in the region from 600 to 200 cm −1 are strongly coupled with the side‐chain deformation vibrations.
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