Preparation of amyloid fibrils for magic-angle spinning solid-state NMR spectroscopy

Marcus D. Tuttle, Joseph M. Courtney, Alexander M. Barclay, Chad M. Rienstra

Research output: Chapter in Book/Report/Conference proceedingChapter


Solid-state NMR spectroscopy (SSNMR) is an established and invaluable tool for the study of amyloid fibril structure with atomic-level detail. Optimization of the homogeneity and concentration of fibrils enhances the resolution and sensitivity of SSNMR spectra. Here, we present a fibrillization and fibril processing protocol, starting from purified monomeric α-synuclein, that enables the collection of highresolution SSNMR spectra suitable for site-specific structural analysis. This protocol does not rely on any special features of α-synuclein and should be generalizable to any other amyloid protein.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages11
StatePublished - 2016

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Amyloid fibrils
  • Fibrillization
  • Size exclusion chromatography
  • Solid-state NMR
  • α-synuclein

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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