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Proton transverse relaxation as a sensitive probe for structure determination in solid proteins.

MPG-Autoren
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Rovo,  P.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

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Grohe,  K.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

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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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Linser,  R.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

Externe Ressourcen

http://onlinelibrary.wiley.com/doi/10.1002/cphc.201500799/epdf
(Verlagsversion)

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2192675_Suppl.pdf
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Zitation

Rovo, P., Grohe, K., Giller, K., Becker, S., & Linser, R. (2015). Proton transverse relaxation as a sensitive probe for structure determination in solid proteins. ChemPhysChem, 16(18), 3791-3796. doi:10.1002/cphc.201500799.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0028-5B1F-2
Zusammenfassung
Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy has been used successfully to elucidate atomic-resolution structures of insoluble proteins. However, the major bottleneck is the difficulty to obtain valuable long-distance structural information. Here we propose to use distance restraints as long as 32 Å obtained from quantification of transverse proton relaxation induced by a methanethiosulfonate spin label (MTSL). Combined with dipolar proton-proton distance restraints, we are able to obtain a protein structure with excellent precision from a single spin-labeled protein sample of an amount of 1 mg under fast magic angle spinning.