in bacteria and archaea 10% - 15%: in eukarya 5% - 10% %
||Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU. Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem. 201382:323-55. doi: 10.1146/annurev-biochem-060208-092442. p.330 right column 2nd paragraphPubMed ID23746257
||P.330 right column 2nd paragraph: "The chaperonins interact with 10–15% of newly synthesized polypeptides in bacteria and archaea (primary sources 15, 52, 53) and 5–10% in eukarya (primary source 50). The obligate substrates of GroEL typically include proteins with complex domain folds, which tend to populate kinetically trapped folding intermediates (primary sources 15, 53). Established TRiC [tailless complex polypeptide-1 (TCP-1) ring complex (TRiC)] substrates include the cytoskeletal proteins actin and tubulin as well as several proteins with β-propellers/WD40 repeats (ref 49, primary source 50)."