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Molecular chaperone

Introduction: Molecular chaperone

Description of Molecular chaperone

Molecular chaperone: diverse family of prokaryotic and eukaryotic intracellular proteins involved in the assembly and transmembrane translocation of other proteins; seem to function by stabilizing partially unfolded states; includes certain heat shock proteins.
Source: CRISP

Molecular chaperone: A family of cellular proteins that mediate the correct assembly or disassembly of other polypeptides, and in some cases their assembly into oligomeric structures, but which are not components of those final structures. It is believed that chaperone proteins assist polypeptides to self-assemble by inhibiting alternative assembly pathways that produce nonfunctional structures. Some classes of molecular chaperones are the nucleoplasmins, the CHAPERONINS, the HEAT-SHOCK PROTEINS 70, and the HSP90 HEAT-SHOCK PROTEINS.
Source: MeSH 2007

Molecular chaperone: Related Topics

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Source - CRISP

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Source: CRISP

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