Acid‐base properties for each protonation site of six corticotropin fragments

BÉLA NOSZÁL, ERZSÉBET OSZTÁS

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The individual basicity of each protonation site for six different fragments of aH‐ACTH (corticotropin) have been characterized in terms of group constants. Microconstants have also been estimated for the N‐ and C‐terminal moieties of ACTH (15–32) and ACTH (1–28), respectively. In these cases the bifunctional termini contain adjacent protonation sites of similar basicity in close interaction. For fragments consisting of 14 or fewer amino acids the acid‐base properties of all the protonation sites can be well interpreted by taking into account only the primary peptide structure. The group constant values for ACTH (15‐32), ACTH (1‐28) and ACTH (1‐32) provide evidence that the functional groups of these fragments are influenced by several intramolecular interactions such as H‐bonding and macromolecular hydrophobic effects. By means of the above constants the concentration of any arbitrarily chosen microspecies can be calculated.

Original languageEnglish
Pages (from-to)162-166
Number of pages5
JournalInternational journal of peptide and protein research
Volume33
Issue number2
DOIs
Publication statusPublished - Feb 1989

Keywords

  • ACTH
  • acid‐base equilibria
  • corticotrophin
  • dissociation constant
  • group constant
  • microconstant
  • microspeciation
  • protonation isomers
  • submolecular basicity

ASJC Scopus subject areas

  • Biochemistry

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