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

Publisher Website
Google Scholar
Abstract
The conformational properties of an analog of atrial naturiuretic factor, [Pro‐10] ANF(7‐23), were examined in H2O, H2O/DMSO‐d6 (2/1), and DMSO‐d6 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 Overhàuser 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‐10] ANF(7‐23) exhibits a considerable amount of flexibility in all of the solvents employed.