@inbook{75171359248c431b8bad7e27950f4f58,
title = "Preparation of amyloid fibrils for magic-angle spinning solid-state NMR spectroscopy",
abstract = "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.",
keywords = "Amyloid fibrils, Fibrillization, Size exclusion chromatography, Solid-state NMR, α-synuclein",
author = "Tuttle, {Marcus D.} and Courtney, {Joseph M.} and Barclay, {Alexander M.} and Rienstra, {Chad M.}",
note = "Publisher Copyright: {\textcopyright} Springer Science+Business Media New York 2016.",
year = "2016",
doi = "10.1007/978-1-4939-2978-8_11",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "173--183",
booktitle = "Methods in Molecular Biology",
}