Year-end Sale % OFF 
Abstract
The native structure of the protein α-synuclein, which is implicated in Parkinson's disease, is controversial. In-cell nuclear magnetic resonance now shows that it remains disordered when loaded into living cells. See Article p.45 Amyloid aggregates of the protein α-synuclein are associated with Parkinson's disease and although the isolated protein is disordered in vitro, various conformations have been proposed for the protein in its physiological context in vivo, ranging from disordered monomers to folded helical tetramers. Now, using atomic-resolution in-cell NMR and EPR spectroscopy, Philipp Selenko and colleagues show that α-synuclein remains disordered within all mammalian cells tested, including neurons, and identify which parts of the protein dynamically interact with, or remain shielded from the cytoplasm, thus preventing aggregation in physiological conditions. The study presents several experimental methods applied for the first time to a protein inside mammalian cells.
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
