Abstract
USA Understanding the mechanisms and pathways of protein folding constitutes a problem of fundamental biological significance. It has been known for more than three decades that all the information required for the acqisition of the native state is contained in the linear amino acid sequence of the polypeptide chain. Proteins are capable of spontaneous folding in the test-tube, at least under carefully chosen conditions, and this has led to the view that also within cells newly-synthesized polypeptides reach their native state in an essentially spontaneous reaction. Only more recently has it been realized that this is not generally the case. Cells contain a complex machinery of proteins, folding catalysts and so-called molecular chaperones, which mediate folding in the cytosol as well as within subcellular compartments such as mitochondria, chloroplasts and the endoplasmic reticulum (Hendrick and Hartl, 1993; Hard et al. , 1994; Hartl and Martin, 1995). Molecular chaperones, mostly constitutively expressed stress proteins, play a preeminent role in these processes and are the main focus of this chapter.
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Hartl, FU. (1996). Protein Folding In The Cell: The Role Of Molecular Chaperones. In: Op den Kamp, J.A.F. (eds) Molecular Dynamics of Biomembranes. NATO ASI Series, vol 96. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61126-1_8
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DOI: https://doi.org/10.1007/978-3-642-61126-1_8
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