The heat shock protein Hsp20 family, also known as small heat shock proteins (sHSPs), is a family of heat shock proteins. Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp). Amongst them is a family of proteins with an average molecular weight of 20 kDa, known as the hsp20 proteins. These seem to act as protein chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Structurally, this family is characterised by the presence of a conserved C-terminal domain, alpha-crystallin domain, of about 100 residues. Recently, small heat shock proteins (sHSPs) were found in marine
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| - The heat shock protein Hsp20 family, also known as small heat shock proteins (sHSPs), is a family of heat shock proteins. Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp). Amongst them is a family of proteins with an average molecular weight of 20 kDa, known as the hsp20 proteins. These seem to act as protein chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Structurally, this family is characterised by the presence of a conserved C-terminal domain, alpha-crystallin domain, of about 100 residues. Recently, small heat shock proteins (sHSPs) were found in marine (en)
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| - Hsp20/alpha crystallin family (en)
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| - The heat shock protein Hsp20 family, also known as small heat shock proteins (sHSPs), is a family of heat shock proteins. Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp). Amongst them is a family of proteins with an average molecular weight of 20 kDa, known as the hsp20 proteins. These seem to act as protein chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Structurally, this family is characterised by the presence of a conserved C-terminal domain, alpha-crystallin domain, of about 100 residues. Recently, small heat shock proteins (sHSPs) were found in marine viruses (cyanophages). (en)
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| - I:47-137 A:47-150 F:46-147 (en)
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