Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins

Daniela Lalli; Paul Schanda; Anup Chowdhury; Joren Retel; Matthias Hiller; Victoria A. Higman; Lieselotte Handel; Vipin Agarwal; Bernd Reif; Barth Van Rossum; Ümit Akbey; Hartmut Oschkinat

doi:10.1007/s10858-011-9578-1

Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins

Daniela Lalli, Paul Schanda, Anup Chowdhury, Joren Retel, Matthias Hiller, Victoria A. Higman, Lieselotte Handel, Vipin Agarwal, Bernd Reif, Barth Van Rossum, Ümit Akbey, Hartmut Oschkinat

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Abstract

Well-resolved ²H-¹³C correlation spectra, reminiscent of ¹H-¹³C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of ²H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T ₁, allowing for high repetition rates and enabling 3D experiments with a ²H-¹³C transfer step in a reasonable time. Well-resolved 3D ²H_DQ-¹³C-¹³C correlations of ubiquitin and OmpG were recorded within 3.5 days each. An essentially complete assignment of ²H_DQα shifts and of a substantial fraction of ²H_DQβ shifts were obtained for ubiquitin. In the case of OmpG, ²H_DQα and ²H_DQβ chemical shifts of a considerable number of threonine, serine and leucine residues were assigned. This approach provides the basis for a general heteronuclear 3D MAS NMR assignment concept utilizing pulse sequences with ²H_DQ-¹³C transfer steps and evolution of deuterium double-quantum chemical shifts.

Original language	English
Pages (from-to)	477-485
Number of pages	9
Journal	Journal of Biomolecular NMR
Volume	51
Issue number	4
DOIs	https://doi.org/10.1007/s10858-011-9578-1
Publication status	Published - Dec 2011
Externally published	Yes

Keywords

Deuterium-carbon correlations
Membrane proteins
Micro-crystalline
OmpG
Solid-state NMR
Ubiquitin

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10.1007/s10858-011-9578-1

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Lalli, D., Schanda, P., Chowdhury, A., Retel, J., Hiller, M., Higman, V. A., Handel, L., Agarwal, V., Reif, B., Van Rossum, B., Akbey, Ü., & Oschkinat, H. (2011). Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal of Biomolecular NMR, 51(4), 477-485. https://doi.org/10.1007/s10858-011-9578-1

@article{1302d60cca3c48cda05b28cdc3916640,

title = "Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins",

abstract = "Well-resolved 2H-13C correlation spectra, reminiscent of 1H-13C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of 2H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T 1, allowing for high repetition rates and enabling 3D experiments with a 2H-13C transfer step in a reasonable time. Well-resolved 3D 2HDQ-13C-13C correlations of ubiquitin and OmpG were recorded within 3.5 days each. An essentially complete assignment of 2HDQα shifts and of a substantial fraction of 2HDQβ shifts were obtained for ubiquitin. In the case of OmpG, 2HDQα and 2HDQβ chemical shifts of a considerable number of threonine, serine and leucine residues were assigned. This approach provides the basis for a general heteronuclear 3D MAS NMR assignment concept utilizing pulse sequences with 2HDQ-13C transfer steps and evolution of deuterium double-quantum chemical shifts.",

keywords = "Deuterium-carbon correlations, Membrane proteins, Micro-crystalline, OmpG, Solid-state NMR, Ubiquitin",

author = "Daniela Lalli and Paul Schanda and Anup Chowdhury and Joren Retel and Matthias Hiller and Higman, {Victoria A.} and Lieselotte Handel and Vipin Agarwal and Bernd Reif and {Van Rossum}, Barth and {\"U}mit Akbey and Hartmut Oschkinat",

note = "Funding Information: Acknowledgments Prof. Beat H. Meier is gratefully acknowledged for the measurement time provided at the 600 MHz magnet at ETH Z{\"u}rich. AC and JR gratefully acknowledge Marie Cruie FP7-ITN (SBMP) funding (grant number 211800).",

year = "2011",

month = dec,

doi = "10.1007/s10858-011-9578-1",

language = "English",

volume = "51",

pages = "477--485",

journal = "Journal of Biomolecular NMR",

issn = "0925-2738",

publisher = "Springer Science and Business Media B.V.",

number = "4",

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Lalli, D, Schanda, P, Chowdhury, A, Retel, J, Hiller, M, Higman, VA, Handel, L, Agarwal, V, Reif, B, Van Rossum, B, Akbey, Ü & Oschkinat, H 2011, 'Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins', Journal of Biomolecular NMR, vol. 51, no. 4, pp. 477-485. https://doi.org/10.1007/s10858-011-9578-1

TY - JOUR

T1 - Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins

AU - Lalli, Daniela

AU - Schanda, Paul

AU - Chowdhury, Anup

AU - Retel, Joren

AU - Hiller, Matthias

AU - Higman, Victoria A.

AU - Handel, Lieselotte

AU - Agarwal, Vipin

AU - Reif, Bernd

AU - Van Rossum, Barth

AU - Akbey, Ümit

AU - Oschkinat, Hartmut

N1 - Funding Information: Acknowledgments Prof. Beat H. Meier is gratefully acknowledged for the measurement time provided at the 600 MHz magnet at ETH Zürich. AC and JR gratefully acknowledge Marie Cruie FP7-ITN (SBMP) funding (grant number 211800).

PY - 2011/12

Y1 - 2011/12

N2 - Well-resolved 2H-13C correlation spectra, reminiscent of 1H-13C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of 2H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T 1, allowing for high repetition rates and enabling 3D experiments with a 2H-13C transfer step in a reasonable time. Well-resolved 3D 2HDQ-13C-13C correlations of ubiquitin and OmpG were recorded within 3.5 days each. An essentially complete assignment of 2HDQα shifts and of a substantial fraction of 2HDQβ shifts were obtained for ubiquitin. In the case of OmpG, 2HDQα and 2HDQβ chemical shifts of a considerable number of threonine, serine and leucine residues were assigned. This approach provides the basis for a general heteronuclear 3D MAS NMR assignment concept utilizing pulse sequences with 2HDQ-13C transfer steps and evolution of deuterium double-quantum chemical shifts.

AB - Well-resolved 2H-13C correlation spectra, reminiscent of 1H-13C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of 2H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T 1, allowing for high repetition rates and enabling 3D experiments with a 2H-13C transfer step in a reasonable time. Well-resolved 3D 2HDQ-13C-13C correlations of ubiquitin and OmpG were recorded within 3.5 days each. An essentially complete assignment of 2HDQα shifts and of a substantial fraction of 2HDQβ shifts were obtained for ubiquitin. In the case of OmpG, 2HDQα and 2HDQβ chemical shifts of a considerable number of threonine, serine and leucine residues were assigned. This approach provides the basis for a general heteronuclear 3D MAS NMR assignment concept utilizing pulse sequences with 2HDQ-13C transfer steps and evolution of deuterium double-quantum chemical shifts.

KW - Deuterium-carbon correlations

KW - Membrane proteins

KW - Micro-crystalline

KW - OmpG

KW - Solid-state NMR

KW - Ubiquitin

UR - http://www.scopus.com/inward/record.url?scp=84855257903&partnerID=8YFLogxK

U2 - 10.1007/s10858-011-9578-1

DO - 10.1007/s10858-011-9578-1

M3 - Article

SN - 0925-2738

VL - 51

SP - 477

EP - 485

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

IS - 4

ER -

Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins

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Keywords

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