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Journal Article

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;

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

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

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

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Shi,  C.
Research Group of Solid-State NMR, 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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Wolff,  S.
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;

Fulltext (public)

2087008.pdf
(Publisher version), 510KB

Supplementary Material (public)
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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: http://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.