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ChemBioChem

Volumn 11, Issue 14, 2010, Pages 1993-1996

Probing the micelle-bound aggregation-prone state of α-synuclein with19F NMR spectroscopy

(3) Wang, Gui Fang a Li, Conggang a,b Pielak, Gary J a,b

a University of North Carolina at Chapel Hill (United States)

b Wuhan National Laboratory for Optoelectronics (China)

Author keywords

Fluorine; Micelles; NMR spectroscopy; Protein aggregation; Unnatural amino acids

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; FLUORINE NUCLEAR MAGNETIC RESONANCE; MICELLE; NITROGEN NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

ALPHA-SYNUCLEIN; AMINO ACIDS; HALOGENATION; HUMANS; MICELLES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PARKINSON DISEASE; PROTEIN CONFORMATION; PROTEIN UNFOLDING;

EID: 77957196424 PISSN: 14394227 EISSN: 14397633 Source Type: Journal
DOI: 10.1002/cbic.201000405 Document Type: Article

Times cited : (21)

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