Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases

Amyloid fibrils associated with numerous degenerative diseases are non-crystalline and insoluble, and thus are not amenable to conventional X-ray crystallography and solution NMR, the classical tools of structural biology. We have recently demonstrated that deep UV resonance Raman (DUVRR) spectrosco...

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Veröffentlicht in:Current science (Bangalore) 2009-07, Vol.97 (2), p.180-185
Hauptverfasser: Lednev, Igor K., Shashilov, Victor, Xu, Ming
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Shashilov, Victor
Xu, Ming
description Amyloid fibrils associated with numerous degenerative diseases are non-crystalline and insoluble, and thus are not amenable to conventional X-ray crystallography and solution NMR, the classical tools of structural biology. We have recently demonstrated that deep UV resonance Raman (DUVRR) spectroscopy combined with hydrogen–deuterium exchange and advanced statistical analysis, 2D correlation in particular, allow for quantitative characterization of protein structural evolution at all stages of fibrillation in vitro. The application of DUVRR spectroscopy for studying the fibrillation of lysozyme is briefly overviewed here.
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source Free E-Journal (出版社公開部分のみ); JSTOR
subjects Aggregation
Alzheimers disease
Amides
Amyloids
Fibrillation
Prion diseases
Raman scattering
Raman spectroscopy
Solar fibrils
SPECIAL SECTION: RAMAN SPECTROSCOPY
Spectroscopy
title Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases
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