title: [The spatial organization and conformational flexibility of neuropeptides of the gallatostatin family].
abstract: The spatial organization and conformational flexibility of neuropeptides of the gallatostatin family was studied by the method of theoretical conformational analysis. It was found that the spatial organization of neuropeptides allows the realization of folded helical structures of the C-terminal pentapeptide, and the flexibility of neuropeptides is due to a great number of low-energy states in the N-terminal fragment of the molecule.
authors.forename: I N
authors.initials: IN
authors.lastname: Alieva
authors.forename: L I
authors.initials: LI
authors.lastname: Velieva
authors.forename: D I
authors.initials: DI
authors.lastname: Aliev
authors.forename: N M
authors.initials: NM
authors.lastname: Godzhaev
mesh_terms: D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: C096416:Met-callatostatin; D009479:Neuropeptides; C080360:callatostatin