## 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
Use of potentiometric titration for determination of α- and ω-peptide bonds in poly(aspartic acid) and poly(glutamic acid)
✍ Scribed by V. Saudek
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 422 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 critically. An analysis of the equation describing the dependence of pH on the degree of neutralization based on neglecting the polymer effect and a discussion of the dissociation behavior of polyanions show that the method of evaluating experimental data found in the literature is incorrect. Nevertheless, if a conformational transition does not interfere, some useful and reliable information may be gained by this method; namely, an indication of the presence of two different peptide bonds, their mole ratio, and an approximate p__K__ value for the carboxyl of the amino acid linked in the ω‐peptide bond. The presence of two types of carboxyls complicates the evaluation of the titration curves in the conformation studies.
📜 SIMILAR VOLUMES
## 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,