Proton-detected MAS NMR experiments based on dipolar transfers for backbone 
assignment of highly deuterated proteins.

Chevelkov, V.; Habenstein, B.; Loquet, A.; Giller, K.; Becker, S.; Lange, A.

doi:10.1016/j.jmr.2014.02.020

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Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins.

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Chevelkov, V.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons79129

Habenstein, B.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons36494

Loquet, A.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons36496

Giller, K.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker, S.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lange, A.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/S1090780714000718/pdfft?md5=029b8987e3cb843c6014ce963468c430&pid=1-s2.0-S1090780714000718-main.pdf
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Citation

Chevelkov, V., Habenstein, B., Loquet, A., Giller, K., Becker, S., & Lange, A. (2014). Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins. Journal of Magnetic Resonance, 242, 180-188. doi:10.1016/j.jmr.2014.02.020.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-8BC4-9

Abstract

Proton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system (T3SS) needle. Spectra of very high resolution and sensitivity were obtained at a low protonation level of 10-20% at exchangeable amide positions. We developed efficient experimental protocols for resonance assignment tailored for this system and the employed experimental conditions. Using exclusively dipolar-based interspin magnetization transfers, we recorded two sets of 3D spectra allowing for an almost complete backbone resonance assignment of the needle subunit PrgI. The additional information provided by the well-resolved proton dimension revealed the presence of two sets of resonances in the N-terminal helix of PrgI, while in previous studies employing 13C detection only a single set of resonances was observed.