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Volumn 64, Issue 4, 2002, Pages 221-226
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Structural transformation and aggregation of human α-synuclein in trifluoroethanol: Non-amyloid component sequence is essential and β-sheet formation is prerequisite to aggregation
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Author keywords
synuclein; sheet; Aggregation; Non amyloid component segment; Trifluoroethanol
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Indexed keywords
DISEASES;
HYDROPHOBICITY;
PATHOGENESIS;
PROTEINS;
8 ANILINO 1 NAPHTHALENESULFONIC ACID;
ALPHA SYNUCLEIN;
TRIFLUOROETHANOL;
ALPHA HELIX;
AMINO ACID SEQUENCE;
ARTICLE;
BETA SHEET;
CARBOXY TERMINAL SEQUENCE;
CONFORMATIONAL TRANSITION;
HUMAN;
HYDROPHOBICITY;
PARKINSON DISEASE;
PATHOGENESIS;
PROTEIN AGGREGATION;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STRUCTURE;
SEQUENCE ANALYSIS;
STRUCTURE ACTIVITY RELATION;
STRUCTURE ANALYSIS;
ALPHA-SYNUCLEIN;
BIOPOLYMERS;
CIRCULAR DICHROISM;
GAMMA-SYNUCLEIN;
HUMANS;
MACROMOLECULAR SUBSTANCES;
NERVE TISSUE PROTEINS;
PARKINSON DISEASE;
PEPTIDE FRAGMENTS;
PROTEIN STRUCTURE, SECONDARY;
SPECTROMETRY, FLUORESCENCE;
SYNUCLEINS;
TRIFLUOROETHANOL;
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EID: 0037025817
PISSN: 00063525
EISSN: None
Source Type: Journal
DOI: 10.1002/bip.10179 Document Type: Article |
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Times cited : (72)
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References (21)
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