| chaperone | <cell biology> 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. (18 Nov 1997) |
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accompany as a chaperone chaperon: one who accompanies and supervises a young woman or gatherings of young people
Ãâó: wordnet.princeton.edu/perl/webwn
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| chaperone |
(chap
Ãâó: www.mercksource.com/pp/us/cns/cns_hl_dorlands.jspz...
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| chaperone |
Newly synthesized proteins must fold into a particular three-dimensional conformation, which is an extremely difficult process that most proteins fail to accomplish. Folding is assisted by chaperone proteins that bind and stabilize folding intermediates.
Ãâó: www.nature.com/nri/journal/v5/n6/glossary/nri1635_...
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| chaperone |
Any of a class of proteins that helps proteins fold or escorts proteins or other molecules throughout the cell.
Ãâó: www.nigms.nih.gov/news/science_ed/chemhealth/gloss...
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| chaperone |
A protein that helps other proteins to fold up into their correct 3D structure.
Ãâó: xray.bmc.uu.se/~kenth/bioinfo/glossary.html
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| chaperone | one who accompanies and supervises a young woman or gatherings of young people |
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| chaperone | accompany as a chaperone |
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