020: Біологія та екологія

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Temperature dependet conformational changes in tertiary structure of alpha-crystallin molecular chaperone from eye lens
(2002) Vadzyuk, Olga
Tryptophan ultra-violet fluorescence and flиorescеnt probes were used to study conformational changes ofalpha-crystallin in a broad temperature range from 0 to 60 C. We observed steady and almost linearshift of ultra-violet fluorescence spectra to longer wavelengths at the increase of temperature. This shift was accompanied by only a small reduction of red-edge effect, which witnessesfor the maintenance of the rigidity in protein structure at the sites of location of tryptophan residues, even at high temperatures. Fluorescence of bound probe 8-anilino-1 naphtalene sulfonate demonstrates temperature-dependent increase of hydro-phobicity of the oligomer surface, which correlates with the increasing of ability toprevent the aggregation of the denatured insulin. Our results indicate that the conformational changes in alpha-crystallin tertiary structure occur with increasing of temperature and they are responsible for the increasing chaperone activity of alpha-crystallin.