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Viscosity and potentiometric measurements of poly( L ‐histidyl‐ L ‐alanyl‐α‐ L ‐glutamic acid) and poly( L ‐lysyl‐ L ‐alanyl‐α‐ L ‐glutamic acid)
Author(s) -
Goren H. Joseph,
Grandan Loretta,
Jay Alfred W. L.,
Lotan Noah
Publication year - 1977
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.1977.360160713
Subject(s) - potentiometric titration , chemistry , glutamic acid , salt (chemistry) , viscosity , polymer , titration , intrinsic viscosity , polymer chemistry , side chain , amino acid residue , amino acid , organic chemistry , biochemistry , peptide sequence , thermodynamics , ion , physics , gene
Poly(His‐Ala‐Glu) and poly(Lys‐Ala‐Glu) were examined by viscosity and potentiometric titration. These measurements were interpreted in terms of the hydrodynamic size of the above sequential polypeptides. Effects of polymer, size and concentration, and solution‐salt concentration were demonstrated. Although the sequential polypeptides generally behave like polyampholytes, they do demonstrate some differences. These differences my be attributed to the ability of ionized side chains three residues apart to repel themselves, in the order His < Glu < Lys.