title: [Thermodynamic basis for the water-bridge structure of collagen].
abstract: A solution of the problem of topology of hydrogen bond net in a triple-helix of collagen is suggested on the basis of thermodynamic data on denaturation of phylogenetically different collagen, as well as on that of the earlier evaluation of the energy of OH-group 4-hydroxyproline bond. It is shown that only water-bridged collagen structure in the variant of Ramachandran school can explain both the change of thermal stability upon the extent of proline hydroxylation and the phylogenetic change of thermostability.
authors.forename: T V
authors.initials: TV
authors.lastname: Burdzhanadze
mesh_terms: D003094:Collagen / Q000737:chemistry* / Q000235:genetics; D006860:Hydrogen Bonding; D006909:Hydroxyproline / Q000737:chemistry; D008433:Mathematics; D010802:Phylogeny; D011487:Protein Conformation; D011489:Protein Denaturation; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D014867:Water; D003094:Collagen; D006909:Hydroxyproline
vernacular_title: Termodinamicheskoe obosnovanie vodno-mostikovoĭ struktury kollagena.