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13C-Nmr studies of ACTH: Assignment of resonances and conformational features

✍ Scribed by Flavio Toma; Serge Fermandjian; Miklos Löw; Lajos Kisfaludy

Book ID
102765136
Publisher
Wiley (John Wiley & Sons)
Year
1981
Tongue
English
Weight
706 KB
Volume
20
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The biologically active ACTH(1–32) and ACTH(1–24) and other shorter peptide segments of the native hormone ACTH(1–39) were studied in aqueous solution by ^13^C‐nmr. In order to identify the ^13^C resonances—except those of the carbonyls—both high‐field nmr spectroscopy measurements and substitution of residues with amino acids enriched to 85% in ^13^C were carried out. The main results are (1) the direct characterization of the cis–trans isomerism of proline 24 and its effects on the directly connected and sequentially neighboring residues and (2) findings that the conformational features agree with an α‐helix type organization in the N‐terminal part of the ACTH molecule which is responsible for the biological activity.

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