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3D MAS NMR Experiment Utilizing Through-Space 15N–15N Correlations

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† Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States
§ Department of Biochemistry and Structural Biology, Lund University, Lund 221 00, Sweden
*[email protected]
Cite this: J. Am. Chem. Soc. 2017, 139, 19, 6518–6521
Publication Date (Web):April 27, 2017
https://doi.org/10.1021/jacs.7b01159
Copyright © 2017 American Chemical Society
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    Abstract

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    We demonstrate a novel 3D NNC magic angle spinning NMR experiment that generates 15N–15N internuclear contacts in protein systems using an optimized 15N–15N proton assisted recoupling (PAR) mixing period and a 13C dimension for improved resolution. The optimized PAR condition permits the acquisition of high signal-to-noise 3D data that enables backbone chemical shift assignments using a strategy that is complementary to current schemes. The spectra can also provide distance constraints. The utility of the experiment is demonstrated on an M0Aβ1–42 fibril sample that yields high-quality data that is readily assigned and interpreted. The 3D NNC experiment therefore provides a powerful platform for solid-state protein studies and is broadly applicable to a variety of systems and experimental conditions.

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