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Title High-sensitivity rheo-NMR spectroscopy for protein studies
Date 30.06.2017
Number 52901
Abstract Shear stress can induce structural deformation of proteins, which might result in aggregate formation. Rheo-NMR spectroscopy has the potential to monitor structural changes in proteins under shear stress at the atomic level; however, existing Rheo-NMR methodologies have insufficient sensitivity to probe protein structure and dynamics. Here we present a simple and versatile approach to Rheo-NMR, which maximizes sensitivity by using a spectrometer equipped with a cryogenic probe. As a result, the sensitivity of the instrument ranks highest among the Rheo-NMR spectrometers reported so far. We demonstrate that the newly developed Rheo-NMR instrument can acquire high-quality relaxation data for a protein under shear stress and can trace structural changes in a protein during fibril formation in real time. The described approach will facilitate rheological studies on protein structural deformation, thereby aiding a physical understanding of shear-induced amyloid fibril formation.
URL http://dx.doi.org/10.1021/acs.analchem.7b01816
Publisher Analytical Chemistry
Identifier 0
Citation Analytical Chemistry 89 (2017) 7286-7290
DOI http://dx.doi.org/10.1021/acs.analchem.7b01816
Authors Morimoto, D. ; Walinda, E. ; Iwakawa, N. ; Nishizawa, M. ; Kawata, Y. ; Yamamoto, A. ; Shirakawa, M. ; Scheler, U. ; Sugase, K.
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