High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies

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Date
2017
Volume
89
Issue
14
Journal
Analytical chemistry : the authoritative voice of the analytical community
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Publisher
Columbus, Ohio : American Chemical Society
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.

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Morimoto, D., Walinda, E., Iwakawa, N., Nishizawa, M., Kawata, Y., Yamamoto, A., et al. (2017). High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies (Columbus, Ohio : American Chemical Society). Columbus, Ohio : American Chemical Society. https://doi.org//10.1021/acs.analchem.7b01816
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