Coordination-chemical study of polypeptides, III protonation-deprotonation equilibrium study of synthetic αH-corticotropin1-32. Data on the pH-dependent conformation of corticotropin

K. Burger, F. Gaizer, B. Noszál, M. Pékli, G. Takácsi-Nagy

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Abstract

By potentiometric equilibrium measurements and the computer evaluation of experimental data, the protonation equilibrium constants of four fragments of corticotropin (ACTH), ACTH1-32, ACTH1-28, ACTH1-14 and ACTH1-4, were determined and assigned to the corresponding functional groups. From the dependence of the protonation constants on the length of the peptide chain, it was established which functional groups participate in the formation of intramolecular hydrogen-bonds in aqueous solutions at various pH. These results indicated a pH-dependent conformation of the molecule.

Original languageEnglish
Pages (from-to)335-344
Number of pages10
JournalBioinorganic Chemistry
Volume7
Issue number4
DOIs
Publication statusPublished - 1977

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Deprotonation
Protonation
Adrenocorticotropic Hormone
Functional groups
Conformations
Peptides
Equilibrium constants
Hydrogen
Hydrogen bonds
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)

Cite this

Coordination-chemical study of polypeptides, III protonation-deprotonation equilibrium study of synthetic αH-corticotropin1-32. Data on the pH-dependent conformation of corticotropin. / Burger, K.; Gaizer, F.; Noszál, B.; Pékli, M.; Takácsi-Nagy, G.

In: Bioinorganic Chemistry, Vol. 7, No. 4, 1977, p. 335-344.

Research output: Contribution to journalArticle

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