Biologically Active Substance
molecular chaperone
[ muh-lek-yuh-ler shap-uh-rohn ]
Subclass of:
Proteins
Definitions related to molecular chaperones:
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(chaperone) Cytoplasmic proteins of both prokaryotes and eukaryotes that bind to nascent or unfolded polypeptides and ensure correct folding or transport. Chaperone proteins do not covalently bind to their targets and do not form part of the finished product. Heat-shock proteins are an important sub set of chaperones. Three major families are recognised, the chaperonins (groEL and hsp60), the hsp70 family and the hsp90 family. Outside these major families are other proteins with similar functions including nucleoplasmin, secB and T-cell receptor associated protein.NCI ThesaurusU.S. National Cancer Institute, 2021
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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.CRISP ThesaurusNational Institutes of Health, 2006
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A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.NLM Medical Subject HeadingsU.S. National Library of Medicine, 2021
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