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Solid‐state conformation of copolymers of β‐benzyl‐ L ‐aspartate with L ‐alanine, L ‐leucine, L ‐valine, γ‐benzyl‐ L ‐glutamate, or ϵ‐carbobenzoxy‐ L ‐lysine
Author(s) -
Sederel Willem L.,
Bantjes Adriaan,
Feijen Jan,
Anderson James M.
Publication year - 1980
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.1980.360190905
Subject(s) - chemistry , valine , alanine , copolymer , monomer , leucine , amide , stereochemistry , circular dichroism , lysine , optical rotatory dispersion , helix (gastropod) , amino acid , polymer , organic chemistry , biochemistry , ecology , snail , biology
The solid‐state conformation of copolymers of β‐benzyl‐ L ‐aspartate [ L ‐Asp(OBzl)] with L ‐leucine ( L ‐Leu), L ‐alanine ( L ‐Ala), L ‐valine ( L ‐Val), γ‐benzyl‐ L ‐glutamate [ L ‐Glu(OBzl)], or ϵ‐carbobenzoxy‐ L ‐lysine (Cbz‐ L ‐Lys) has been studied by ir spectroscopy and circular dichroism (CD). The ir spectra in the region of the amide I and II bands and in the region of 700–250 cm −1 have been determined. The results from the ir studies are in good agreement with data obtained by CD experiments. Incorporation of the amino acid residues mentioned above into poly[ L ‐Asp(OBzl)] induces a change from the left‐handed into the right‐handed α‐helix. This conformational change for the poly[ L ‐Asp(OBzl)] copolymers was observed in the following composition ranges: L ‐Leu, 0–15 mol %; L ‐Ala, 0–32 mol %; L ‐Val, 0–8 mol %; L ‐Glu(OBzl), 3–10 mol %; and Cbz‐ L ‐Lys, 0–9 mol %.