[Structuro-functional organization of delta sleep-inducing peptide].

Theoretical conformational analysis was carried out for a nonapeptide hormone (delta sleep-inducing peptide). Possible structure of the neuropeptide under physiological conditions may be described by a set of low-energy conformations belonging to nine different forms of the backbone. A solution of the "reverse conformational problem" for delta sleep inducing peptide enables one to predict modified amino acid sequences (D-Ala3-, Pro4-, Pro6-, Pro7, and Tyr7-analogs), which may assume one of the low-energy states of the native hormone. The influence of the solute was not taken into account in our calculations.