| Literature DB >> 31311708 |
Abstract
In this perspective article I briefly highlight the rapid progress made over the past two decades in atomic level structural and dynamic studies of amyloids, which are representative of non-crystalline biomacromolecular assemblies, by magic-angle spinning solid-state NMR spectroscopy. Given new and continuing developments in solid-state NMR instrumentation and methodology, ongoing research in this area promises to contribute to an improved understanding of amyloid structure, polymorphism, interactions, assembly mechanisms, and biological function and toxicity.Entities:
Keywords: Amyloid fibrils; Magic-angle spinning; Protein structure and dynamics; Solid-state NMR
Year: 2019 PMID: 31311708 PMCID: PMC6703944 DOI: 10.1016/j.jmr.2019.07.015
Source DB: PubMed Journal: J Magn Reson ISSN: 1090-7807 Impact factor: 2.229