NMR paper Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization.

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[NMR paper] Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization.

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NMR assignment:

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NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

Refinement:

Amber

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Fragment-based:

Homology-based:

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Promega- Proline

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TALOS

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Methyl S2

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MAXOCC

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01-31-2015, 04:16 PM

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Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization.

Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization.

Related Articles Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization.

J Biomol NMR. 2015 Jan 30;

Authors: Chevelkov V, Xiang S, Giller K, Becker S, Lange A, Reif B

Abstract
In this work, we show how the water flip-back approach that is widely employed in solution-state NMR can be adapted to proton-detected MAS solid-state NMR of highly deuterated proteins. The scheme allows to enhance the sensitivity of the experiment by decreasing the recovery time of the proton longitudinal magnetization. The method relies on polarization transfer from non-saturated water to the protein during the inter-scan delay.

PMID: 25634300 [PubMed - as supplied by publisher]

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