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Helix–coil transition in copolypeptides. II. Poly(γ‐benzyl L ‐glutamate‐ co ‐ε‐carbobenzoxy‐ L ‐lysine)
Author(s) -
Roig A.,
Blanco F. García,
Cortijo M.
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.360100209
Subject(s) - chemistry , cooperativity , helix (gastropod) , solvent , lysine , polymer , transition (genetics) , polymer chemistry , stereochemistry , organic chemistry , amino acid , biochemistry , ecology , snail , gene , biology
The thermal helix–coil transition of poly(γ‐benzyl L ‐glutamate‐ co ‐ε‐carbobenzoxy‐ L ‐lysine) copolypeptides was studied in solvent mixtures of different compositions. The cooperativity parameter v changes linearly with polymer (and solvent) composition, whereas the heat of the transition shows a very pronounced minimum as a function of polymer composition. This minimum cannot be due only or mainly to the solvent changes and must be attributed to the effect on the transition of the side chains of the polypeptides.