Lysine residues in the N-terminal huntingtin amphipathic α-helix play a key role in peptide aggregation

Journal of Mass Spectrometry

Volumn 50, Issue 1, 2015, Pages 117-126

  Arndt, James R ^a   Brown, Robert J ^a   Burke, Kathleen A ^a   Legleiter, Justin ^a   Valentine, Stephen J ^a  

^a WEST VIRGINIA UNIVERSITY   (United States)

Author keywords

Amphipathic alpha helix; Atomic force microscopy; Huntington's disease; Hydrogen deuterium exchange; Thioflavin T fluorescence assay

Indexed keywords

AGGREGATES; AMINO ACIDS; ATOMIC FORCE MICROSCOPY; DEUTERIUM; DISSOCIATION; ELECTRON TRANSITIONS; ELECTROSPRAY IONIZATION; HYDROGEN; MASS SPECTROMETRY; PEPTIDES; PROTEINS; SPECTROMETRY;

AGGREGATION KINETICS; ALPHA HELIX; ELECTRON TRANSFER DISSOCIATION; FLUORESCENCE ASSAY; HUNTINGTON'S DISEASE; HYDROGEN-DEUTERIUM EXCHANGE; NEURODEGENERATIVE DISORDERS; TANDEM MASS SPECTROMETRY;

NEURODEGENERATIVE DISEASES;

GLUTAMINE; HUNTINGTIN; LYSINE; HTT PROTEIN, HUMAN; NERVE PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; DEUTERIUM HYDROGEN EXCHANGE; DNA FLANKING REGION; ELECTRON TRANSPORT; ELECTROSPRAY; KINETICS; MORPHOLOGY; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; PROTEOMICS; TANDEM MASS SPECTROMETRY; ATOMIC FORCE MICROSCOPY; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; PROCEDURES; PROTEIN SECONDARY STRUCTURE;

DEUTERIUM EXCHANGE MEASUREMENT; HYDROGEN-ION CONCENTRATION; LYSINE; MICROSCOPY, ATOMIC FORCE; NERVE TISSUE PROTEINS; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TANDEM MASS SPECTROMETRY;

EID: 84921649003     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.3504     Document Type: Article

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