title: [Changes in the secondary structure bacteriophage T4 envelope protein after its polymerization].
abstract: Circular dichroism (CD) spectra of the structural protein of the bacteriophage T4 sheath (gp 18) in a monomeric native state, helices, polysheaths and contracted sheaths were measured in the range 184-310 nm. The secondary structure of the protein studied was calculated from the spectra in the range 190-240 nm according to Provencher and Glöckner. It has been shown that the polymerization is proceeded without change of the alpha-helical content in the secondary structure of gp 18: estimated alpha-helix in monomeric gp 18, helices and polysheaths was 39%. The beta-form content in monomeric gp 18, helices and polysheaths was 33, 32 and 37%, respectively. Tail sheath contraction is attended by a 14% decrease in gp 18 alpha-helicity and a 5% increase in its beta-form content.
authors.forename: I I
authors.initials: II
authors.lastname: Serysheva
authors.forename: S Iu
authors.initials: SIu
authors.lastname: Ven'iaminov
authors.forename: N A
authors.initials: NA
authors.lastname: Selivanov
authors.forename: L P
authors.initials: LP
authors.lastname: Rodikova
authors.forename: B F
authors.initials: BF
authors.lastname: Poglazov
mesh_terms: D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D011108:Polymers; D011487:Protein Conformation; D013604:T-Phages / Q000032:analysis* / Q000648:ultrastructure; D014759:Viral Envelope Proteins / Q000032:analysis* / Q000648:ultrastructure
chemical_list: D011108:Polymers; D014759:Viral Envelope Proteins
vernacular_title: Izmenenie vtorichnoĭ struktury dlia polimerizatsii chekhol'nogo belka bakteriofaga T4.