Study of α-crystallin structure by small angle neutron scattering with contrast variation

A. V. Krivandin, T. N. Murugova, A. I. Kuklin, K. O. Muranov, N. B. Poliansky, V. L. Aksenov, M. A. Ostrovsky

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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 molec-ular weight substances) should be taken into account when elaborating α-crystallin quaternary structure models.

Original languageEnglish
Pages (from-to)1324-1330
Number of pages7
JournalBiochemistry (Moscow)
Volume75
Issue number11
DOIs
Publication statusPublished - Nov 1 2010

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Keywords

  • Contrast variation
  • Quaternary structure
  • Small-angle neutron scattering
  • α-crystallin

ASJC Scopus subject areas

  • Biochemistry

Cite this

Krivandin, A. V., Murugova, T. N., Kuklin, A. I., Muranov, K. O., Poliansky, N. B., Aksenov, V. L., & Ostrovsky, M. A. (2010). Study of α-crystallin structure by small angle neutron scattering with contrast variation. Biochemistry (Moscow), 75(11), 1324-1330. https://doi.org/10.1134/S0006297910110039