[The structural transformations of X-oligomers].
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.
Rozenfel'd
M A
MA
Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
Kostanova
E A
EA
Vasil'eva
M V
MV
Leonova
V B
VB
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
D005338:Fibrin Fibrinogen Degradation Products; D011108:Polymers; C030568:fibrinogen fragment X; D005340:Fibrinogen