| Literature DB >> 26453214 |
Asher Moshe1, Meytal Landau1, David Eisenberg2.
Abstract
The molecular structures of amyloid fibers and oligomers are required in order to understand and control their formation. Yet, their partially disordered and polymorphic nature hinders structural analyses. Fortunately, short segments from amyloid proteins, which exhibit similar biophysical properties to the full-length proteins, also form fibrils and oligomers and their atomic structures can be determined. Here we describe experimental procedures used to assess fiber-forming capabilities of amyloid peptide segments and their crystallization.Entities:
Keywords: Amyloid-like peptides; Cross-β spine; Cylindrin; Microcrystallography; Microcrystals; Steric zipper
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Year: 2016 PMID: 26453214 DOI: 10.1007/978-1-4939-2978-8_13
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745