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• W76714253 abstract "The propensity of proteins or peptides to misfold into amyloid deposits is associated with many neurodegenerative and systemic amyloid related diseases. It was originally thought that information stored in a polypeptide chain encodes only a single native fold. The transition of a protein from its soluble functional form into the β-sheet-rich insoluble ordered filamentous polymer is a special form of misfolding which poses a great intellectual challenge to the scientific community which seeks to understand the underlying mechanism. It is now believed that amyloid fibrillation may be a separate alternative folding pathway. This process is not unique to any specific class of proteins and appears to be an alternative conformation of the polypeptide backbone, in which fibrillation conditions are dictated by the amino acid sequence. Unlike native protein folding, in fibrillation, a single polypeptide chain can produce polymorphic fibrils that differ in intra- or inter-residue interactions, and which result in variations of filament number, arrangement and conformation. In this chapter we survey all the α-helical proteins that have been shown to undergo this transition to the amyloid-like form. Moreover, we discuss the unique polymorphisms that may be associated with each α-helical protein, and advances in our understanding of the transition of helical proteins into amyloid fibrils." @default.
• W76714253 created "2016-06-24" @default.
• W76714253 creator A5059576369 @default.
• W76714253 creator A5077885102 @default.
• W76714253 date "2014-01-01" @default.
• W76714253 modified "2023-09-24" @default.
• W76714253 title "Conversion of α-Helical Proteins into an Alternative β-Amyloid Fibril Conformation" @default.
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• W76714253 doi "https://doi.org/10.1016/b978-0-12-394431-3.00043-2" @default.
• W76714253 hasPublicationYear "2014" @default.
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