Acid‐base properties for each protonation site of six corticotropin fragments
- 1 February 1989
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 33 (2) , 162-166
- https://doi.org/10.1111/j.1399-3011.1989.tb00202.x
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.Keywords
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