Biopolym. Cell. 1988; 4(3):139-144, 150.
Structure and Function of Biopolymers
Hydrodynamic characteristics of the 12S-oligomer of the protein of inclusion bodies of a nuclear polyhedrosis virus of the silkworm (Bombyx mori)
1Lylo V. V., 2Serebryani S. B.
  1. Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR
  2. Institute of Organic Chemistry, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR

Abstract

The molecular weight of the polyhedral protein was obtained by two techniques: sedimentation equilibrium (M=333000 Da) and sedimentation-diffusion (M = 344000 Da). Itshyd-rodynamic characteristics (sedimentation constant s020, w = 11.9 S and diffusion constant D020, w = 3.2·10–7 cm2/g) were determined as well. Frictional and axial ratios of protein molecules approximated by ellipsoids of revolution were calculated by the data obtained earlier for the monomer and in this work for the oligomer. Taking account of the protein partial solvation the monomer has a semiaxis ratio of 13 and the oligomer has also an asymmetrical shape with a semiaxis ratio of 4.5. The model of 12 monomer molecules packing in one oligomer molecule, similar to a keratin model, is suggested.

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