[Structure-functional organization of the secretin molecule. II. Direct conformation problem].
Spatial structure of peptide hormone secretin was investigated by the theoretical conformational method. A solution of the "direct conformational problem" for this hormone indicated that the possible structure of the secretin molecule under polar conditions may be described only by two families of low-energy conformations, possessing relatively conformational valid (Thr7-Leu22) and variable (His1-Phe6 and Leu23-Val27NH2) fragments. One of these families is comprised by five twists of the alpha-helix, while the second isoenergetic family possesses two short segments of the alpha-helix, divided by an irregular structure of the tetrapeptide.
D000595:Amino Acid Sequence; D006801:Humans; D008954:Models, Biological; D009842:Oligopeptides; D011487:Protein Conformation; D012633:Secretin / Q000031:analogs & derivatives; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D012633:Secretin
Strukturno-funktsional'naia organizatsiia molekuly sekretina. II. Priamaia strukturnaia zadacha.