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Article

Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors.

The Journal of biological chemistry - 8 Mar 2013

Sarell Claire J, Woods Lucy A, Su Yongchao, Debelouchina Galia T, Ashcroft Alison E, Griffin Robert G, Stockley Peter G, Radford Sheena E

Abstract excerpt

Amyloid fibrils can be generated from proteins with diverse sequences and folds. Although amyloid fibrils assembled in vitro commonly involve a single protein precursor, fibrils formed in vivo can contain more than one protein sequence. How fibril structure and stability differ in fibrils composed of single proteins (homopolymeric fibrils) from those generated by co-polymerization of more than one protein...

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Share to Amyloid
Share to beta 2-Microglobulin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Hydrophobic and Hydrophilic Interactions

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Identifiers

PMID: 23329840
DOI: 10.1074/jbc.M112.447524
PMCID: PMC3591641

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