Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour

Nature Communications

Volumn 5, Issue , 2014, Pages

  Fusco, Giuliana ^a   De Simone, Alfonso ^b   Gopinath, Tata ^c   Vostrikov, Vitaly ^c   Vendruscolo, Michele ^a   Dobson, Christopher M ^a   Veglia, Gianluigi ^c  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

^c UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; LIPID; LIPID BILAYER; LIPOSOME; PROTEIN BINDING;

LIPID; MEMBRANE; NERVOUS SYSTEM DISORDER; NUCLEAR MAGNETIC RESONANCE; PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; LIPID MEMBRANE; MEMBRANE BINDING; MOLECULAR DYNAMICS; NITROGEN NUCLEAR MAGNETIC RESONANCE; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SOLID STATE; SYNAPSE VESICLE; BIOLOGICAL MODEL; CELL MEMBRANE; CHEMISTRY; LIPID BILAYER; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE;

ALPHA-SYNUCLEIN; CELL MEMBRANE; LIPID BILAYERS; LIPIDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; UNILAMELLAR LIPOSOMES;

EID: 84901812732     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4827     Document Type: Article

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