Small heat shock proteins (sHsps) are a widespread and diverse class of molecular chaperones that bind non-native proteins in an ATP-independent manner. They form oligomer ensembles and a shift to smaller oligomers is usually required for chaperone activation. Caenorhabditis elegans encodes 16 different sHsps, among them Hsp17. This sHsp has a unique structural organization, chaperone function and in vivo expression pattern. Moreover, two sHsps had been identified in Chaetomium thermophilum and characterized concerning their structural and functional features.
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Small heat shock proteins (sHsps) are a widespread and diverse class of molecular chaperones that bind non-native proteins in an ATP-independent manner. They form oligomer ensembles and a shift to smaller oligomers is usually required for chaperone activation. Caenorhabditis elegans encodes 16 different sHsps, among them Hsp17. This sHsp has a unique structural organization, chaperone function and in vivo expression pattern. Moreover, two sHsps had been identified in Chaetomium thermophilum and...
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