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• W2177409077 startingPage "149" @default.
• W2177409077 abstract "1H-detection offers a substitute to the sensitivity-starved experiments often used to characterize biomolecular samples using magic-angle spinning solid-state NMR spectroscopy (MAS-ssNMR). To mitigate the effects of the strong 1H–1H dipolar coupled network that would otherwise severely broaden resonances, high MAS frequencies (>40 kHz) are often employed. Here, we have explored the alternative of stroboscopic 1H-detection at moderate MAS frequencies of 5–30 kHz using windowed version of supercycled-phase-modulated Lee-Goldburg homonuclear decoupling. We show that improved resolution in the 1H dimension, comparable to that obtainable at high spinning frequencies of 40–60 kHz without homonuclear decoupling, can be obtained in these experiments for fully protonated proteins. Along with detailed analysis of the performance of the method on the standard tri-peptide f-MLF, experiments on micro-crystalline GB1 and amyloid-β aggregates are used to demonstrate the applicability of these pulse-sequences to challenging biomolecular systems. With only two parameters to optimize, broadbanded performance of the homonuclear decoupling sequence, linear dependence of the chemical-shift scaling factor on resonance offset and a straightforward implementation under experimental conditions currently used for many biomolecular studies (viz. spinning frequencies and radio-frequency amplitudes), we expect these experiments to complement the current 13C-detection based methods in assignments and characterization through chemical-shift mapping." @default.
• W2177409077 created "2016-06-24" @default.
• W2177409077 creator A5009181212 @default.
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• W2177409077 date "2015-12-01" @default.
• W2177409077 modified "2023-09-25" @default.
• W2177409077 title "Proton-detected solid-state NMR spectroscopy of fully protonated proteins at slow to moderate magic-angle spinning frequencies" @default.
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• W2177409077 doi "https://doi.org/10.1016/j.jmr.2015.10.016" @default.
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