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Conformational studies on polypeptides. The effect of sodium perchlorate on the conformation of poly‐ L ‐lysine and of random copolymers of L ‐lysine and L ‐phenylalanine in aqueous solution
Author(s) -
Peggion E.,
Cosani A.,
Terbojevich M.,
Borin G.
Publication year - 1972
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.1972.360110308
Subject(s) - chemistry , lysine , circular dichroism , copolymer , phenylalanine , protonation , amino acid , side chain , sodium perchlorate , stereochemistry , polymer chemistry , polymer , ion , crystallography , biochemistry , organic chemistry , electrode , electrochemistry
Circular Dichroism measurements have been carried out on poly‐ L ‐lysine (PLL) and on random copolymers of lysine and phenylalanine at various p H values and in the presence of different amounts of NaClO 4 . The results indicate that either the homopolymer or the copolymers at p H conditions at which the side‐chain amino groups are fully protonated, assume the right‐handed α‐helical conformation in the presence of NaClO 4 . The results are interpreted in terms of specific binding of ClO 4 − ions on charged side‐chain amino groups.