title: [Conformation of a triple collagen spiral as a function of primary structure].
abstract: It has been shown by the method of conformational analysis that conformation of the polypeptide chain of a collagen molecule varies from one type of sequence to another, but in all the sequences the only two types of conformations can be characterized by minimal conformational energy. The collagen molecule as a whole is a combination of the single-bond Rich and Crick model and new double-bonded structure. Rigorous comparison with "thick" conformations obtained by Scheraga and coworkers was undertaken using precise calculations with flexible proline.
authors.forename: V G
authors.initials: VG
authors.lastname: Tumanian
authors.forename: V N
authors.initials: VN
authors.lastname: Rogulenkova
authors.forename: N G
authors.initials: NG
authors.lastname: Esipova
authors.forename: F
authors.initials: F
authors.lastname: Aĭzenkhaber
mesh_terms: D000595:Amino Acid Sequence; D003094:Collagen / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D003094:Collagen
vernacular_title: Konformatsiia troĭnoĭ spirali kollagena kak funktsiia pervichnoĭ struktury.