Electron paramagnetic resonance spectroscopy measures the distance between the external β-strands of folded α-synuclein in amyloid fibrils

Biophysical Journal

Volumn 101, Issue 1, 2011, Pages L1-L3

  Karyagina, Irina ^a   Becker, Stefan ^a   Giller, Karin ^a   Riedel, Dietmar ^a   Jovin, Thomas M ^a   Griesinger, Christian ^a,b   Bennati, Marina ^a,b  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; MUTANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ELECTRON SPIN RESONANCE; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; AMYLOID; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 80052474665     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.05.052     Document Type: Article

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