![]() It has 24 subunits, each with an immunoglobulin fold, arranged as a hollow shell with holes. The structure of an archaebacterial small heat shock protein. Main role: They prevent inappropriate association or aggregation of exposed hydrophobic surfaces and direct their substrates into productive folding, transport or degradation pathways. Essential for viability, their expression is often increased by cellular stress.They often couple ATP binding/hydrolysis to the folding process.Some chaperones are non-specific, and interact with a wide variety of polypeptide chains, but others are restricted to specific targets.They do not interact with native proteins, nor do they form part of the final folded structures. ![]()
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