Journal
METHODS
Volume 148, Issue -, Pages 123-135Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2018.04.015
Keywords
Solid-state NMR; Dynamics; Structural biology; Protein aggregation; Membrane proteins
Funding
- National Institutes of Health [R01 AG019322, R01 GM112678, R01 GM113908]
- National Institutes of Health S10 grant [OD012213-01]
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Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural characterization of a diverse array of biological assemblies that include amyloid fibrils, non-amyloid aggregates, membrane-associated proteins and viral capsids. Such biological samples feature functionally relevant molecular dynamics, which often affect different parts of the sample in different ways. Solid-state NMR experiments' sensitivity to dynamics represents a double-edged sword. On the one hand, it offers a chance to measure dynamics in great detail. On the other hand, certain types of motion lead to signal loss and experimental inefficiencies that at first glance interfere with the application of ssNMR to overly dynamic proteins. Dynamics-based spectral editing (DYSE) ssNMR methods leverage motion-dependent signal losses to simplify spectra and enable the study of substructures with particular motional properties.
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