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

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3D MAS NMR Experiment Utilizing Through-Space 15N-15N Correlations. / Donovan, Kevin J.; Silvers, Robert; Linse, Sara; Griffin, Robert G.

I: Journal of the American Chemical Society, Vol. 139, Nr. 19, 17.05.2017, s. 6518-6521.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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Donovan, Kevin J. ; Silvers, Robert ; Linse, Sara ; Griffin, Robert G. / 3D MAS NMR Experiment Utilizing Through-Space 15N-15N Correlations. I: Journal of the American Chemical Society. 2017 ; Vol. 139, Nr. 19. s. 6518-6521.

RIS

TY - JOUR

T1 - 3D MAS NMR Experiment Utilizing Through-Space 15N-15N Correlations

AU - Donovan, Kevin J.

AU - Silvers, Robert

AU - Linse, Sara

AU - Griffin, Robert G

PY - 2017/5/17

Y1 - 2017/5/17

N2 - 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.

AB - 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.

U2 - 10.1021/jacs.7b01159

DO - 10.1021/jacs.7b01159

M3 - Article

VL - 139

SP - 6518

EP - 6521

JO - Journal of the American Chemical Society

T2 - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 1520-5126

IS - 19

ER -