α-synuclein populates both elongated and broken helix states on small unilamellar vesicles

Journal of Biological Chemistry

Volumn 286, Issue 24, 2011, Pages 21450-21457

  Bekshe Lokappa, Sowmya ^a   Ulmer, Tobias S ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENTROPY MEASUREMENT; FREE-ENERGY DIFFERENCE; GEL STATE; HELICAL CONFORMATION; HELIX CONFORMATION; INTERCONVERSIONS; MISFOLDING; MOLECULAR CHAINS; PARKINSON DISEASE; PHYSIOLOGICAL FEATURES; POPULATION RATIO; RANDOM COIL; S STATE; SMALL UNILAMELLAR VESICLE; STRUCTURAL STATE; SYNAPTIC VESICLE; SYNUCLEIN; UPPER LIMITS;

CONFORMATIONS; FREE ENERGY; PHYSIOLOGY;

SYNCHROTRONS;

ALPHA SYNUCLEIN;

ARTICLE; BACTERIAL CELL; CONTROLLED STUDY; ENTHALPY; ENTROPY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; SYNAPSE VESICLE;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; CALORIMETRY; CELL MEMBRANE; CIRCULAR DICHROISM; CYSTEINE; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE; THERMODYNAMICS; UNILAMELLAR LIPOSOMES;

EID: 79958727550     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.224055     Document Type: Article

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