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Updated: Jun 21, 2026

The Lambda Select cII Mutation Detection System
Published on: April 26, 2018
Resistance of alpha-crystallin quaternary structure to UV irradiation
A V Krivandin1, K O Muranov, F Yu Yakovlev
1Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. a.krivandin@sky.chph.ras.ru
Abstract:
The damaging effect of UV radiation (lambda > 260 nm) on bovine alpha-crystallin in solution was studied by small-angle X-ray scattering, gel permeation chromatography, electrophoresis, absorption and fluorescence spectroscopy, and differential scanning calorimetry. The results obtained show that damage to even a large number of subunits within an alpha-crystallin oligomer does not cause significant rearrangement of its quaternary structure, aggregation of oligomers, or the loss of their solubility. Due to the high resistance of its quaternary structure, alpha-crystallin is able to prevent aggregation of destabilized proteins (especially of gamma- and beta-crystallins) and so to maintain lens transparency throughout the life of an animal (the chaperone-like function of alpha-crystallin).
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