Resonance Raman Spectroscopic Measurements Delineate the Structural Changes that Occur during Tau Fibril Formation

The aggregation of the microtubule-associated protein, tau, into amyloid fibrils is a hallmark of neurodegenerative diseases such as the tauopathies and Alzheimer’s disease. Since monomeric tau is an intrinsically disordered protein and the polymeric fibrils possess an ordered cross-β core, the aggr...

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Veröffentlicht in:	Biochemistry (Easton) 2014-10, Vol.53 (41), p.6550-6565
Hauptverfasser:	Ramachandran, Gayathri, Milán-Garcés, Erix A, Udgaonkar, Jayant B, Puranik, Mrinalini
Format:	Artikel
Sprache:	eng
Schlagworte:	Amyloid - chemistry Amyloid - genetics Amyloid - metabolism Amyloid - ultrastructure Fluorescent Dyes Heparin - chemistry Heparin - metabolism Humans Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - genetics Intrinsically Disordered Proteins - metabolism Intrinsically Disordered Proteins - ultrastructure Kinetics Microscopy, Atomic Force Models, Molecular Protein Aggregation, Pathological Protein Conformation Protein Interaction Domains and Motifs Protein Stability Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Repetitive Sequences, Amino Acid Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Spectrum Analysis, Raman tau Proteins - chemistry tau Proteins - genetics tau Proteins - metabolism tau Proteins - ultrastructure Thiazoles - chemistry
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