Structural heterogeneity in microcrystalline ubiquitin studied by solid-state 
NMR.

Fasshuber, H. K.; Lakomek, N. A.; Habenstein, B.; Loquet, A.; Shi, C.; Giller, K.; Wolff, S.; Becker, S.; Lange, A.

doi:10.1002/pro.2654

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Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.

MPS-Authors

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Fasshuber, H. K.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15409

Lakomek, N. A.
Department of NMR Based Structural Biology, 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/persons130763

Shi, C.
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;

/persons/resource/persons71888

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

/persons/resource/persons14824

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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Citation

Fasshuber, H. K., Lakomek, N. A., Habenstein, B., Loquet, A., Shi, C., Giller, K., et al. (2015). Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR. Protein Science, 24(5), 592-598. doi:10.1002/pro.2654.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-B39A-9

Abstract

By applying [1-13 C]- and [2-13 C]-glucose labeling schemes to the folded globular protein ubiquitin, a strong reduction of spectral crowding and increase in resolution in solid-state NMR (ssNMR) spectra could be achieved. This allowed spectral resonance assignment in a straightforward manner and the collection of a wealth of long-range distance information. A high precision solid-state NMR structure of microcrystalline ubiquitin was calculated with a backbone rmsd of 1.57 to the X-ray structure and 1.32 Å to the solution NMR structure. Interestingly, we can resolve structural heterogeneity as the presence of three slightly different conformations. Structural heterogeneity is most significant for the loop regions β1-β2 but also for β-strands β1, β2, β3 and β5 as well as for the loop connecting α1 and β3. This structural polymorphism observed in the solid-state NMR spectra coincides with regions that showed dynamics in solution NMR experiments on different timescales. This article is protected by copyright. All rights reserved.