Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain

FEBS Letters

Volumn 587, Issue 16, 2013, Pages 2572-2577

  Wietek, Jonas ^a   Haralampiev, Ivan ^a   Amoussouvi, Aouefa ^a   Herrmann, Andreas ^a   Stöckl, Martin ^a,b  

^a HUMBOLDT UNIVERSITY   (Germany)

^b UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

alpha synuclein; Fluorescence spectroscopy; Lipid bilayer; Penetration depth

Indexed keywords

ALPHA SYNUCLEIN; AMINO ACID; TRYPTOPHAN;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; EMBEDDING; LIPID BILAYER; MEMBRANE BINDING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

ALPHA-SYNUCLEIN; FLUORESCENCE SPECTROSCOPY; LIPID BILAYER; PENETRATION DEPTH;

ACRYLAMIDE; ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; CELL MEMBRANE; HUMANS; LIPID BILAYERS; LIPIDS; MICELLES; MOLECULAR SEQUENCE DATA; PARKINSON DISEASE; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLSERINES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; TRYPTOPHAN;

EID: 84881477828     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.06.034     Document Type: Article

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