title: Spatial organization and conformational peculiarities of the callatostatin family of neuropeptides.
abstract: The structures and conformational peculiarities of five members of the callatostatin family of neuropeptides, i.e. Leu- and Met-callatostatins, ranging in size from 8 to 16 amino acid residues have been investigated by a theoretical conformational analysis method. A comparative analysis of the conformational flexibilities of Met-callatostatin with those of the hydroxylated analogues, [Hyp2]- and [Hyp3]-Met-callatostatin has been carried out. Helically packed C-terminal pentapeptide in the structure of all investigated Leu-callatostatins are shown to be possible. The reason for the great number low-energy conformers for the callatostatin N-terminus is discussed.
authors.affiliation: Laboratory of Molecular Biophysics, Baku State University, Azerbaijan Republic.
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: Alie
authors.forename: N M
authors.initials: NM
authors.lastname: Godjaev
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003198:Computer Simulation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D013816:Thermodynamics
chemical_list: D009479:Neuropeptides; D009842:Oligopeptides; D010446:Peptide Fragments; C080360:callatostatin