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Converging concepts of protein folding in vitro and in vivo



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P R OT E I N F O L D I N G REVIEW Converging concepts of protein folding in vitro and in vivo 2009 Nature America Inc All rights reserved F Ulrich Hartl Manajit Hayer Hartl Most proteins must fold into precise three dimensional conformations to fulfill their biological functions Here we review recent concepts emerging from studies of protein folding in vitro and in vivo with a focus on how proteins navigate the complex folding energy landscape inside cells with the aid of molecular chaperones Understanding these reactions is also of considerable medical relevance as the aggregation of misfolding proteins that escape the cellular quality control machinery underlies a range of debilitating diseases including many age onset neurodegenerative disorders Numerous proteins have been shown to fold spontaneously in vitro confirming Anfinsen s pioneering insight that the linear sequence of the polypeptide chain contains all the necessary information to specify a protein s three dimensional structure1 Although protein folding has been studied intensely for almost 50 years how the final fold and the folding process is determined by the amino acid sequence remains one of the most important problems in biology Moreover in the more recent past it has become clear that in the cell a large fraction of newly synthesized proteins require assistance by molecular chaperones to reach their folded states efficiently and on a biologically relevant timescale2 Clearly proteins in the test tube and in the cell are subject to the same laws of physics so what is special about folding under cellular conditions and why are chaperones necessary The increasing availability of highly sensitive biophysical techniques to study folding in vitro and in cellular systems is now providing new insights into these issues see the Review by Bartlett and Radford3 in this issue These studies also shed light on the process of aggregation a potentially dangerous off pathway reaction that can cause disease and must



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