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Nmr study of poly(aspartic acid). I. α‐ and β‐Peptide bonds in poly(aspartic acid) prepared by thermal polycondensation
Author(s) -
Pivcová H.,
Saudek V.,
Drobník J.,
Vlasák J.
Publication year - 1981
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.1981.360200804
Subject(s) - aspartic acid , condensation polymer , chemistry , peptide bond , peptide , polymer , polymer chemistry , amino acid , organic chemistry , biochemistry
The structure of poly(aspartic acid) prepared by thermal polycondensation has been studied by means of nmr spectroscopy. The analysis of the 13 C‐nmr spectra of the polymer at various pH values and comparison with the spectrum of poly(α‐ L ‐aspartic acid) revealed that the polymer contained aspartic acid linked in α‐ and β‐peptide bonds. The mole fraction of the β‐peptide bonds has been found to be 0.8 ± 0.1. The significance of the results for the evolutionary theory of S. W. Fox is mentioned.