The folding of a protein from a sequence of amino acids to a well-defined tertiary structure is one of the most studied and enigmatic events to take place in biological systems. Relatively recently, it has been established that some proteins and peptides are able to take on conformations other than their native fold to form long fibres known as amyloid. In vivo, these are associated with misfolding diseases, such as Alzheimer's disease, Type 2 diabetes and the amyloidoses. In vitro, peptide assembly leads to amyloid-like fibres that have high stability, resistance to degradation and high tensile strength. Remarkably, despite the lack of any obvious sequence similarity between these fibrillogenic proteins and peptides, all amyloid fibrils share common structural characteristics and their underlying structure is known as ‘cross-β’. Nature is rich in β-sheet protein assemblies such as spider silk and other ‘useful’ amyloids such as curli from Escherichia coli, where the strength of fibrils is fundamental to their function.
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August 2009
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Conference Article|
July 22 2009
Structural integrity of β-sheet assembly
Karen E. Marshall;
Karen E. Marshall
1Department of Chemistry and Biochemistry, School of Life Sciences, University of Sussex, Falmer BN1 9QG, U.K.
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Louise C. Serpell
Louise C. Serpell
1
1Department of Chemistry and Biochemistry, School of Life Sciences, University of Sussex, Falmer BN1 9QG, U.K.
1To whom correspondence should be addressed (email L.C.Serpell@sussex.ac.uk).
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Publisher: Portland Press Ltd
Received:
February 26 2009
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem Soc Trans (2009) 37 (4): 671–676.
Article history
Received:
February 26 2009
Citation
Karen E. Marshall, Louise C. Serpell; Structural integrity of β-sheet assembly. Biochem Soc Trans 1 August 2009; 37 (4): 671–676. doi: https://doi.org/10.1042/BST0370671
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