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Heat shock protein hsp-16.2 is a small heat shock protein (smHSP) of approximately 16 kDa found in Caenorhabditis elegans. It is expressed only under stress conditions and forms large oligomeric complexes that function as molecular chaperones by binding to unfolded or denatured proteins, thereby preventing their aggregation. HSP16.2 contains a conserved alpha-crystallin domain essential for its oligomerization and chaperone function. Unlike major human drug targets, HSP16.2 is primarily a model for studying the heat shock response, proteostasis, and cellular stress, and is not considered a direct therapeutic target[1][2][3][4].
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