Purification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity

Biochemistry

Volumn 54, Issue 2, 2015, Pages 279-292

  Luth, Eric S ^a   Bartels, Tim ^a   Dettmer, Ulf ^a   Kim, Nora C ^a   Selkoe, Dennis J ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BLOOD; BRAIN; CHROMATOGRAPHY; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; HYDROPHOBICITY; ION EXCHANGE; OLIGOMERS; PHYSIOLOGY; PROTEINS; RECOMBINANT PROTEINS;

AMMONIUM SULFATE PRECIPITATION; GEL FILTRATION; HELICAL CONTENT; HUMAN CORTEX; HUMAN ERYTHROCYTES; HYDROPHOBIC INTERACTIONS; PARKINSON'S DISEASE; STRUCTURE-FUNCTION RELATIONSHIP;

PURIFICATION;

ALPHA SYNUCLEIN; AMMONIUM SULFATE; BETA SYNUCLEIN; POLYMER; TETRAMER;

ACETYLATION; ALPHA HELIX; ARTICLE; BRAIN CORTEX; CIRCULAR DICHROISM; CONTROLLED STUDY; DEPOLYMERIZATION; GRAY MATTER; HUMAN; HUMAN TISSUE; HYDROPHOBICITY; ION EXCHANGE; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN PURIFICATION; WESTERN BLOTTING; WHITE MATTER; BRAIN CHEMISTRY; CHEMISTRY; ION EXCHANGE CHROMATOGRAPHY; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; PRECIPITATION; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SIZE EXCLUSION CHROMATOGRAPHY;

ALPHA-SYNUCLEIN; BETA-SYNUCLEIN; BRAIN CHEMISTRY; CHEMICAL PRECIPITATION; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, ION EXCHANGE; CIRCULAR DICHROISM; HUMANS; MASS SPECTROMETRY; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY;

EID: 84922479429     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501188a     Document Type: Article

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