High-resolution double-quantum deuterium magic angle spinning solid-state NMR spectroscopy of perdeuterated proteins

Vipin Agarwal; Katja Faelber; Peter Schmieder; Bernd Reif

doi:10.1021/ja803620r

High-resolution double-quantum deuterium magic angle spinning solid-state NMR spectroscopy of perdeuterated proteins

Vipin Agarwal, Katja Faelber, Peter Schmieder, Bernd Reif

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

32 Scopus citations

Abstract

We show in this manuscript that ²H,¹³C correlation spectra in uniformly ²H,¹³C isotopically enriched peptides and proteins can be recorded in MAS solid-state NMR with site specific resolution. A resolved deuterium dimension is obtained by evolving ²H double-quantum coherences. Experimental ²H line widths are obtained that are as small as 16 Hz (0.17 ppm at 600 MHz) in the double-quantum dimension. The unprecedented resolution in the deuterium dimension obtained for proteins opens new perspectives for correlation experiments and, in particular, for the characterization of dynamics of proteins in the solid-state.

Original language	English
Pages (from-to)	2-3
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	131
Issue number	1
DOIs	https://doi.org/10.1021/ja803620r
State	Published - 14 Jan 2009
Externally published	Yes

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abstract = "We show in this manuscript that 2H,13C correlation spectra in uniformly 2H,13C isotopically enriched peptides and proteins can be recorded in MAS solid-state NMR with site specific resolution. A resolved deuterium dimension is obtained by evolving 2H double-quantum coherences. Experimental 2H line widths are obtained that are as small as 16 Hz (0.17 ppm at 600 MHz) in the double-quantum dimension. The unprecedented resolution in the deuterium dimension obtained for proteins opens new perspectives for correlation experiments and, in particular, for the characterization of dynamics of proteins in the solid-state.",

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AU - Faelber, Katja

AU - Schmieder, Peter

AU - Reif, Bernd

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Y1 - 2009/1/14

N2 - We show in this manuscript that 2H,13C correlation spectra in uniformly 2H,13C isotopically enriched peptides and proteins can be recorded in MAS solid-state NMR with site specific resolution. A resolved deuterium dimension is obtained by evolving 2H double-quantum coherences. Experimental 2H line widths are obtained that are as small as 16 Hz (0.17 ppm at 600 MHz) in the double-quantum dimension. The unprecedented resolution in the deuterium dimension obtained for proteins opens new perspectives for correlation experiments and, in particular, for the characterization of dynamics of proteins in the solid-state.

AB - We show in this manuscript that 2H,13C correlation spectra in uniformly 2H,13C isotopically enriched peptides and proteins can be recorded in MAS solid-state NMR with site specific resolution. A resolved deuterium dimension is obtained by evolving 2H double-quantum coherences. Experimental 2H line widths are obtained that are as small as 16 Hz (0.17 ppm at 600 MHz) in the double-quantum dimension. The unprecedented resolution in the deuterium dimension obtained for proteins opens new perspectives for correlation experiments and, in particular, for the characterization of dynamics of proteins in the solid-state.

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High-resolution double-quantum deuterium magic angle spinning solid-state NMR spectroscopy of perdeuterated proteins

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