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- Title
Study of α-Crystallin Structure by Small Angle Neutron Scattering with Contrast Variation.
- Authors
Krivandin, A.; Murugova, T.; Kuklin, A.; Muranov, K.; Poliansky, N.; Aksenov, V.; Ostrovsky, M.
- 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% DO) and its average scattering length density at this point (2.4•1010 cm) 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.
- Subjects
CRYSTALLOGRAPHY; NEUTRON scattering; MOLECULAR structure; CRYSTALLOIDS (Botany); DISTRIBUTION (Probability theory); PENETRATION mechanics; POLYPEPTIDES; WATER
- Publication
Biochemistry (00062979), 2010, Vol 75, Issue 11, p1324
- ISSN
0006-2979
- Publication type
Article
- DOI
10.1134/S0006297910110039