## 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 contai
Nmr study of poly(aspartic acid). II. α- and β-Peptide bonds in poly(aspartic acid) prepared by common methods
✍ Scribed by V. Saudek; H. Pivcová; J. Drobník
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 460 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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, contained aspartic acid linked in both α‐ and β‐peptide bonds. The purest polymer, having practically undetectable amounts of β‐bond, was prepared by debenzylation by HBr in trifluoroacetic acid. It was established that the β‐bonds are formed via succinimides.
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## 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
## Abstract The dielectric absorption of poly‐DL‐phenylalanine and poly‐γ‐benzyl‐L‐aspartate (PLAB) was measured in very dilute solutions to determine the type of molecular association and to locate the helix–coil transition. Both polypeptides were present as associated helices in chloroform. The m