title: [Amphiphilic properties of angiotensin and its fragments].
abstract: Many biologically active peptides are supposed to interact with specific receptors mainly due to hydrophobic forces. In order to obtain a more detailed information about the peptide molecule behavior at the "water-non-polar-phase" boundary an approach to the calculation of stable conformations on such a boundary has been developed. This approach is used for investigation of the amphiphilic properties of angiotensin and its six fragments. The results of calculations of transfer energies of these peptides from the water environment to the phase boundary are in agreement with the experimental data.
authors.forename: S G
authors.initials: SG
authors.lastname: Galaktionov
authors.forename: V M
authors.initials: VM
authors.lastname: Tseĭtin
authors.forename: I A
authors.initials: IA
authors.lastname: Vakser
authors.forename: E V
authors.initials: EV
authors.lastname: Prokhorchik
mesh_terms: D000804:Angiotensin II; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008958:Models, Molecular; D010446:Peptide Fragments; D011487:Protein Conformation
chemical_list: D010446:Peptide Fragments; D000804:Angiotensin II
vernacular_title: Amfifil'nye svoĭstva angiotenzina i ego fragmentov.