Role of HSP60 in Folding/Assembly of Mitochondrial Proteins
It has long been believed that polypeptides in the intact cell assume their biologically active conformations through steps of spontaneous folding (Anfinsen, 1973). A host of in vitro experiments support such behaviour, demonstrating refolding of proteins diluted from urea or guanidine into their biologically active forms (e. g., Sela et al., 1957; Garel et al., 1876). Yet the time required for such reactions is often hours or days, in contrast with only minutes required to produce biologically active polypeptides in intact cells. Further, the concentrations of polypeptide at which one can observe refolding in vitro are usually less than those present in the intact cell. Additionally, only certain proteins can undergo refolding in vitro: in general, proteins with complex domain structure and multiple subunits fail to fold in vitro.
KeywordsHydrolysis Glycerol Maize Urea Polypeptide
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