Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins, thus preventing aggregation. Newly made proteins usually must fold from a linear chain of amino acids into a three-dimensional form. Chaperonins belong to a large class of molecules that assist protein folding, called molecular chaperones. The en...
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http://en.wikipedia.org/wiki/Chaperonin
<cell biology> Subset of chaperone proteins found in prokaryotes, mitochondria and plastids major example is prokaryotic GroEL (the eukaryotic equivalent of which is hsp60). ... (18 Nov 1997) ...
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http://www.encyclo.co.uk/local/20973
Type: Term Pronunciation: shap-ĕr-ō′nin Definitions: 1. A molecular complex composed of multiple heat shock protein subunits that assemble into double ring structures. Chaperonins function within the cytoplasm to refold damaged proteins.
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http://www.medilexicon.com/medicaldictionary.php?t=16525
No exact match found.
