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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-B39A-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-0E81-7
Genre: Journal Article

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 Creators:
Fasshuber, H. K.1, Author              
Lakomek, N. A.2, Author              
Habenstein, B.1, Author              
Loquet, A.1, Author              
Shi, C.1, Author              
Giller, K.2, Author              
Wolff, S.2, Author              
Becker, S.2, Author              
Lange, A.2, Author              
Affiliations:
1Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society, ou_persistent35              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: 13C sparse labeling; dynamics; heterogeneity; solid-state NMR; ubiquitin
 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.

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Language(s): eng - English
 Dates: 2015-03-162015-05
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/pro.2654
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Title: Protein Science
Source Genre: Journal
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Pages: - Volume / Issue: 24 (5) Sequence Number: - Start / End Page: 592 - 598 Identifier: -