The mode of α-synuclein binding to membranes depends on lipid composition and lipid to protein ratio

FEBS Letters

Volumn 585, Issue 22, 2011, Pages 3513-3519

  Shvadchak, Volodymyr V ^a   Yushchenko, Dmytro A ^a,b   Pievo, Roberta ^a   Jovin, Thomas M ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b CARNEGIE MELLON UNIVERSITY   (United States)

Author keywords

Environment sensitive dye; EPR; ESIPT; Fluorescence; Protein conformation

Indexed keywords

ALPHA SYNUCLEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; ARTIFICIAL MEMBRANE; CALIBRATION; CARBOXY TERMINAL SEQUENCE; CELL POLARITY; CIRCULAR DICHROISM; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; FLUORESCENCE; LIPID BILAYER; LIPID COMPOSITION; MEMBRANE BINDING; MOLECULAR PROBE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; RIGIDITY; STOICHIOMETRY;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; LIPID BILAYERS; MEMBRANES, ARTIFICIAL; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 80855144163     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.10.006     Document Type: Article

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