## Abstract The nature of peptide bonds in poly(aspartic acid) prepared by debenzylation of poly(β‐benzyl‐L‐aspartate) under various conditions has been studied by means of nmr spectroscopy. It was established that the majority of the polymers prepared, as well as the commercially obtained polymer,
Nmr study of poly(aspartic acid). I. α- and β-Peptide bonds in poly(aspartic acid) prepared by thermal polycondensation
✍ Scribed by H. Pivcová; V. Saudek; J. Drobník; J. Vlasák
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 491 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
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.
📜 SIMILAR VOLUMES
## Abstract Polypeptides of dicarboxylic amino acids having the monomer units linked in α‐ and ω‐peptide bonds contain two kinds of carboxyls of different acidity. How well potentiometric titration can distinguish these two carboxyls and so characterize the nature of the peptide bonds is evaluated