Abstract
The structure of the oligomeric protein α-crystallin from bovine eye lens was investigated by small-angle neutron scattering (SANS) with contrast variation. Based on the SANS curves, the match point for α-crystallin (43% D2O) and its average scattering length density at this point (2.4•1010 cm-2) were evaluated. The radius of gyration and the distance distri- bution functions for α-crystallin were calculated. On the basis of these calculations, it was concluded that α-crystallin is characterized by homogeneous distribution of scattering density in the domains inaccessible for water penetration, and all polypeptide subunits in α-crystallin oligomers undergo equal deuteration. The latter indicates that all α-crystallin subunits are equally accessible for water and presumably for some other low molecular weight substances. These conclusions on the α-crystallin structure (homogeneous distribution of scattering density and equal accessibility of all subunits for low molecular weight substances) should be taken into account when elaborating a-crystallin quaternary structure models.
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Original Russian Text © A. V. Krivandin, T. N. Murugova, A. I. Kuklin, K. O. Muranov, N. B. Poliansky, V. L. Aksenov, M. A. Ostrovsky, 2010, published in Biokhimiya, 2010, Vol. 75, No. 11, pp. 1499–1507.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM10-151, October 10, 2010.
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Krivandin, A.V., Murugova, T.N., Kuklin, A.I. et al. Study of α-Crystallin Structure by Small Angle Neutron Scattering with Contrast Variation. Biochemistry Moscow 75, 1324–1330 (2010). https://doi.org/10.1134/S0006297910110039
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DOI: https://doi.org/10.1134/S0006297910110039