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Protein folding and misfolding

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Abstract

The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. Folding and unfolding are crucial ways of regulating biological activity and targeting proteins to different cellular locations. Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a wide range of highly debilitating and increasingly prevalent diseases.

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Figure 1: A schematic energy landscape for protein folding.
Figure 2: Regulation of protein folding in the ER.
Figure 3: A schematic representation of the general mechanism of aggregation to form amyloid fibrils.
Figure 4: A unified view of some of the types of structure that can be formed by polypeptide chains.

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Acknowledgements

I should like to thank in particular the Wellcome Trust, the Leverhulme Trust and the UK Research Councils for generous support over many years, without whom my own research activities in this area of science could not have been carried out.

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  1. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK

    Christopher M. Dobson

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Dobson, C. Protein folding and misfolding. Nature 426, 884–890 (2003). https://doi.org/10.1038/nature02261

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