αB-crystallin is a molecular chaperone that prevents the formation of cytotoxic protein aggregates. In this work, different variants of αB-crystallin were characterized concerning structure, dynamics and function to elucidate the mechanism of substrate interaction of αB-crystallin. Binding motifs in substrate proteins were investigated using peptide array experiments. Complementary, the role of α-crystallin in lenses of mouse models of cataract was analyzed. Reversible interactions of α-crystallin with unfolding intermediates are suggested as the mode of action.
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αB-crystallin is a molecular chaperone that prevents the formation of cytotoxic protein aggregates. In this work, different variants of αB-crystallin were characterized concerning structure, dynamics and function to elucidate the mechanism of substrate interaction of αB-crystallin. Binding motifs in substrate proteins were investigated using peptide array experiments. Complementary, the role of α-crystallin in lenses of mouse models of cataract was analyzed. Reversible interactions of α-crystall...
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