Lysine residues in the N-terminal huntingtin amphipathic &#945;-helix play a key role in peptide aggregation.

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

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

Arndt, James R; Brown, Robert J; Burke, Kathleen A; Legleiter, Justin; Valentine, Stephen J.

Affiliation

Arndt JR; C. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV, 26506, USA.

J Mass Spectrom ; 50(1): 117-26, 2015 Jan.

Article in En | MEDLINE | ID: mdl-25601683

Subject(s)

Deuterium Exchange Measurement/methods; Lysine/chemistry; Nerve Tissue Proteins/chemistry; Huntingtin Protein; Hydrogen-Ion Concentration; Microscopy, Atomic Force; Protein Structure, Secondary; Spectrometry, Mass, Electrospray Ionization; Tandem Mass Spectrometry

Key words

Huntington's disease; amphipathic alpha helix; atomic force microscopy; hydrogen-deuterium exchange; thioflavin T fluorescence assay

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Full text: 1 Database: MEDLINE Main subject: Deuterium Exchange Measurement / Lysine / Nerve Tissue Proteins Language: En Year: 2015 Type: Article

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Full text: 1 Database: MEDLINE Main subject: Deuterium Exchange Measurement / Lysine / Nerve Tissue Proteins Language: En Year: 2015 Type: Article