1H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residual solvent suppression

Veniamin Chevelkov; Barth J. Van Rossum; Federica Castellani; Kristina Rehbein; Anne Diehl; Morten Hohwy; Stefan Steuernagel; Frank Engelke; Hartmut Oschkinat; Bernd Reif

doi:10.1021/ja029354b

¹H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residual solvent suppression

Veniamin Chevelkov, Barth J. Van Rossum, Federica Castellani, Kristina Rehbein, Anne Diehl, Morten Hohwy, Stefan Steuernagel, Frank Engelke, Hartmut Oschkinat, Bernd Reif

Associate Professorship of Solid-State NMR spectroscopy

Research output: Contribution to journal › Article › peer-review

127 Scopus citations

Abstract

In this communication, we demonstrate the feasibility of ¹H detection in MAS solid-state NMR for a microcrystalline, uniformly ²H,₁₅N-labeled sample of a SH3 domain of chicken ∞-spectrin, using pulsed field gradients for suppression of water magnetization. Today, B₀ gradients are employed routinely in solution-state NMR for coherence order selection and solvent suppression. We suggest to use gradients to purge water magnetization which cannot be suppressed using conventional water suppression schemes. The achievable gain in sensitivity for ₁H detection is in the order of 5 compared to the ¹⁵N detected version of the experiment (at a MAS rotation frequency of 13.5 kHz). We expect that this labeling concept which achieves high sensitivity due to ¹H detection, in combination with the possibility to measure long range ¹H-¹H distances as we have shown previously, to be a useful tool for the determination of protein structures in the solid state.

Original language	English
Pages (from-to)	7788-7789
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	125
Issue number	26
DOIs	https://doi.org/10.1021/ja029354b
State	Published - 2 Jul 2003

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Chevelkov, V., Van Rossum, B. J., Castellani, F., Rehbein, K., Diehl, A., Hohwy, M., Steuernagel, S., Engelke, F., Oschkinat, H., & Reif, B. (2003). ¹H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residual solvent suppression. Journal of the American Chemical Society, 125(26), 7788-7789. https://doi.org/10.1021/ja029354b

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title = "1H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residual solvent suppression",

abstract = "In this communication, we demonstrate the feasibility of 1H detection in MAS solid-state NMR for a microcrystalline, uniformly 2H,15N-labeled sample of a SH3 domain of chicken ∞-spectrin, using pulsed field gradients for suppression of water magnetization. Today, B0 gradients are employed routinely in solution-state NMR for coherence order selection and solvent suppression. We suggest to use gradients to purge water magnetization which cannot be suppressed using conventional water suppression schemes. The achievable gain in sensitivity for 1H detection is in the order of 5 compared to the 15N detected version of the experiment (at a MAS rotation frequency of 13.5 kHz). We expect that this labeling concept which achieves high sensitivity due to 1H detection, in combination with the possibility to measure long range 1H-1H distances as we have shown previously, to be a useful tool for the determination of protein structures in the solid state.",

author = "Veniamin Chevelkov and {Van Rossum}, {Barth J.} and Federica Castellani and Kristina Rehbein and Anne Diehl and Morten Hohwy and Stefan Steuernagel and Frank Engelke and Hartmut Oschkinat and Bernd Reif",

year = "2003",

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Chevelkov, V, Van Rossum, BJ, Castellani, F, Rehbein, K, Diehl, A, Hohwy, M, Steuernagel, S, Engelke, F, Oschkinat, H & Reif, B 2003, '¹H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residual solvent suppression', Journal of the American Chemical Society, vol. 125, no. 26, pp. 7788-7789. https://doi.org/10.1021/ja029354b

TY - JOUR

T1 - 1H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residual solvent suppression

AU - Chevelkov, Veniamin

AU - Van Rossum, Barth J.

AU - Castellani, Federica

AU - Rehbein, Kristina

AU - Diehl, Anne

AU - Hohwy, Morten

AU - Steuernagel, Stefan

AU - Engelke, Frank

AU - Oschkinat, Hartmut

AU - Reif, Bernd

PY - 2003/7/2

Y1 - 2003/7/2

N2 - In this communication, we demonstrate the feasibility of 1H detection in MAS solid-state NMR for a microcrystalline, uniformly 2H,15N-labeled sample of a SH3 domain of chicken ∞-spectrin, using pulsed field gradients for suppression of water magnetization. Today, B0 gradients are employed routinely in solution-state NMR for coherence order selection and solvent suppression. We suggest to use gradients to purge water magnetization which cannot be suppressed using conventional water suppression schemes. The achievable gain in sensitivity for 1H detection is in the order of 5 compared to the 15N detected version of the experiment (at a MAS rotation frequency of 13.5 kHz). We expect that this labeling concept which achieves high sensitivity due to 1H detection, in combination with the possibility to measure long range 1H-1H distances as we have shown previously, to be a useful tool for the determination of protein structures in the solid state.

AB - In this communication, we demonstrate the feasibility of 1H detection in MAS solid-state NMR for a microcrystalline, uniformly 2H,15N-labeled sample of a SH3 domain of chicken ∞-spectrin, using pulsed field gradients for suppression of water magnetization. Today, B0 gradients are employed routinely in solution-state NMR for coherence order selection and solvent suppression. We suggest to use gradients to purge water magnetization which cannot be suppressed using conventional water suppression schemes. The achievable gain in sensitivity for 1H detection is in the order of 5 compared to the 15N detected version of the experiment (at a MAS rotation frequency of 13.5 kHz). We expect that this labeling concept which achieves high sensitivity due to 1H detection, in combination with the possibility to measure long range 1H-1H distances as we have shown previously, to be a useful tool for the determination of protein structures in the solid state.

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U2 - 10.1021/ja029354b

DO - 10.1021/ja029354b

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AN - SCOPUS:0037527816

SN - 0002-7863

VL - 125

SP - 7788

EP - 7789

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 26

ER -

¹H detection in MAS solid-state NMR spectroscopy of biomacromolecules employing pulsed field gradients for residual solvent suppression

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