Structure and topology of the non-amyloid-β component fragment of human α-synuclein bound to micelles: Implications for the aggregation process

Protein Science

Volumn 15, Issue 6, 2006, Pages 1408-1416

  Bisaglia, Marco ^a   Trolio, Alessandra ^a   Bellanda, Massimo ^a   Bergantino, Elisabetta ^a   Bubacco, Luigi ^a   Mammi, Stefano ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

synuclein; Alzheimer's disease; Micelles; NMR; Non amyloid component; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN;

ARTICLE; DNA FLANKING REGION; MICELLIZATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN STRUCTURE; SOLUBILITY;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; CIRCULAR DICHROISM; DETERGENTS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICELLES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PHOSPHORYLCHOLINE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SODIUM DODECYL SULFATE;

EID: 33744500490     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.052048706     Document Type: Article

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