High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies.
High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies.
Anal Chem. 2017 Jun 30;:
Authors: Morimoto D, Walinda E, Iwakawa N, Nishizawa M, Kawata Y, Yamamoto A, Shirakawa M, Scheler U, Sugase K
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.
PMID: 28665116 [PubMed - as supplied by publisher]
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