Abstract
Most current models that describe how polypeptide chains adopt their native three-dimensional structure are based largely upon studies on the refolding of purified denatured proteins in vitro (9,10,13,18). Although these models have provided important insights into protein folding pathways, they have focussed attention primarily upon the spatial organisation of amino acids within the polypeptide chain. It has now become clear that additional factors promote protein folding inside the cell. These include the chaperonins, protein disulphide isomerases and peptidyl prolyl cis-trans isomerases (13-15). In addition, the temporal separation of amino acids during the synthesis of the nascent polypeptide chain might be significant for protein folding in vivo (4, 16, 25).
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Brown, A.J.P., Crombie, T. (1993). mRNA Translation and Protein Folding in vivo . In: Brown, A.J.P., Tuite, M.F., McCarthy, J.E.G. (eds) Protein Synthesis and Targeting in Yeast. NATO ASI Series, vol 71. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-84921-3_35
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DOI: https://doi.org/10.1007/978-3-642-84921-3_35
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