TWGFD

Welcome to Hsp20 !

Hsp20s are ATP-independent molecular chaperones and can form oligomeric protein complexes of 200-800 kDa, which consist of 9 to 50 subunits. Hsp20s possess a conserved structure, consisting of a variable N-terminal region, a more conserved C-terminal region and a C-terminal extension. The more conserved C-terminal region is usually named as the alpha-crystallin domain (ACD), which contains approximately 80 to 100 amino acid residues. Hsp20 can avert protein denaturation, and thus maintain the stability and normal functions of proteins in both eukaryotic and prokaryotic cells. Hsp20 plays an important role in plant heat tolerance.