title: [The structural transformations of X-oligomers].
abstract: Mechanism of self-assembly and the three-dimensional organization of the intermediate soluble forms of X-oligomers in the presence of non-denaturing urea concentration have been studied by dynamic light scattering, analytical ultracentrifugation, and viscometric methods. Swedberg and Kuhn-Mark-Hauwink analysis of the obtained hydrodynamic data accounting the concentration effect on translational friction demonstrated formation of equilibrium single-stranded rod-like protofibrils with end-to-end arrangement of the peripheral domains of X monomers. Upon elongation the single-stranded protofibrils form double-stranded structures through lateral aggregation. We infer that alpha C domains are involved in neither stabilization of the single-stranded structures nor their dimerization.
authors.affiliation: Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
authors.forename: M A
authors.initials: MA
authors.lastname: Rozenfel'd
authors.forename: E A
authors.initials: EA
authors.lastname: Kostanova
authors.forename: M V
authors.initials: MV
authors.lastname: Vasil'eva
authors.forename: V B
authors.initials: VB
authors.lastname: Leonova
mesh_terms: D000818:Animals; D002417:Cattle; D004058:Diffusion; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry; D005340:Fibrinogen / Q000737:chemistry; D008027:Light; D011108:Polymers / Q000737:chemistry*; D012542:Scattering, Radiation; D013053:Spectrophotometry / Q000706:statistics & numerical data; D014461:Ultracentrifugation; D014783:Viscosity
chemical_list: D005338:Fibrin Fibrinogen Degradation Products; D011108:Polymers; C030568:fibrinogen fragment X; D005340:Fibrinogen