Two-Dimensional NMR studies of [Pro-10] atrial natriuretic factor [7-23]

✍ Scribed by Robert T. Gampe Jr.; Peter J. Connolly; Todd Rockway; Stephen W. Fesik

• Book ID: 101718924
• Publisher: Wiley (John Wiley & Sons)
• Year: 1988
• Tongue: English
• Weight: 486 KB
• Volume: 27
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360270210

✦ Synopsis

The conformational properties of an analog of atrial naturiuretic factor, [Pro-lo] ANF(7-23), were examined in H,O, H,O/DMSO-d, (2/1), and DMSO-d, using two-dimensional nmr techniques. The sequence differs from the native peptide by the absence of the exocyclic N-and C-terminal residues, and the substitution of a proline for a glycine at position 10-a modification expected to reduce the conformational flexibility of this analog. The backbone proton nmr resonances were assigned from two-dimensional correlated spectroscopy (2D-COSY), relayed COSY, and 2D nuclear Overhauser enhancement (NOE) experiments, and the solution conformation was evaluated from vicinal spin-spin coupling constants and NOE data. Despite the substitution of a proline in the sequence, [Pro-101 ANF(7-23) exhibits a considerable amount of flexibility in all of the solvents employed.