Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins

Abstract MAS solid-state NMR is capable of determining structures of protonated solid proteins using proton-detected experiments. These experiments are performed at MAS rotation frequency of around 110 kHz, employing 0.5 mg of material. Here, we compare 1H, 13C correlation spectra obtained from prot...

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Autores principales:	Kai Xue, Riddhiman Sarkar, Carina Motz, Sam Asami, Diana C. Rodriguez Camargo, Venita Decker, Sebastian Wegner, Zdenek Tosner, Bernd Reif
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d086e727126b43d6b7851cd83e778236
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spelling	oai:doaj.org-article:d086e727126b43d6b7851cd83e7782362021-12-02T16:06:07ZLimits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins10.1038/s41598-017-07253-12045-2322https://doaj.org/article/d086e727126b43d6b7851cd83e7782362017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07253-1https://doaj.org/toc/2045-2322Abstract MAS solid-state NMR is capable of determining structures of protonated solid proteins using proton-detected experiments. These experiments are performed at MAS rotation frequency of around 110 kHz, employing 0.5 mg of material. Here, we compare 1H, 13C correlation spectra obtained from protonated and deuterated microcrystalline proteins at MAS rotation frequency of 111 kHz, and show that the spectral quality obtained from deuterated samples is superior to those acquired using protonated samples in terms of resolution and sensitivity. In comparison to protonated samples, spectra obtained from deuterated samples yield a gain in resolution on the order of 3 and 2 in the proton and carbon dimensions, respectively. Additionally, the spectrum from the deuterated sample yields approximately 2–3 times more sensitivity compared to the spectrum of a protonated sample. This gain could be further increased by a factor of 2 by making use of stereospecific precursors for biosynthesis. Although the overall resolution and sensitivity of 1H, 13C correlation spectra obtained using protonated solid samples with rotation frequencies on the order of 110 kHz is high, the spectral quality is still poor when compared to the deuterated samples. We believe that experiments involving large protein complexes in which sensitivity is limiting will benefit from the application of deuteration schemes.Kai XueRiddhiman SarkarCarina MotzSam AsamiDiana C. Rodriguez CamargoVenita DeckerSebastian WegnerZdenek TosnerBernd ReifNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kai Xue Riddhiman Sarkar Carina Motz Sam Asami Diana C. Rodriguez Camargo Venita Decker Sebastian Wegner Zdenek Tosner Bernd Reif Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins
description	Abstract MAS solid-state NMR is capable of determining structures of protonated solid proteins using proton-detected experiments. These experiments are performed at MAS rotation frequency of around 110 kHz, employing 0.5 mg of material. Here, we compare 1H, 13C correlation spectra obtained from protonated and deuterated microcrystalline proteins at MAS rotation frequency of 111 kHz, and show that the spectral quality obtained from deuterated samples is superior to those acquired using protonated samples in terms of resolution and sensitivity. In comparison to protonated samples, spectra obtained from deuterated samples yield a gain in resolution on the order of 3 and 2 in the proton and carbon dimensions, respectively. Additionally, the spectrum from the deuterated sample yields approximately 2–3 times more sensitivity compared to the spectrum of a protonated sample. This gain could be further increased by a factor of 2 by making use of stereospecific precursors for biosynthesis. Although the overall resolution and sensitivity of 1H, 13C correlation spectra obtained using protonated solid samples with rotation frequencies on the order of 110 kHz is high, the spectral quality is still poor when compared to the deuterated samples. We believe that experiments involving large protein complexes in which sensitivity is limiting will benefit from the application of deuteration schemes.
format	article
author	Kai Xue Riddhiman Sarkar Carina Motz Sam Asami Diana C. Rodriguez Camargo Venita Decker Sebastian Wegner Zdenek Tosner Bernd Reif
author_facet	Kai Xue Riddhiman Sarkar Carina Motz Sam Asami Diana C. Rodriguez Camargo Venita Decker Sebastian Wegner Zdenek Tosner Bernd Reif
author_sort	Kai Xue
title	Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins
title_short	Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins
title_full	Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins
title_fullStr	Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins
title_full_unstemmed	Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins
title_sort	limits of resolution and sensitivity of proton detected mas solid-state nmr experiments at 111 khz in deuterated and protonated proteins
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/d086e727126b43d6b7851cd83e778236
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Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins

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