Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR
| dc.contributor.author | FASSHUBER, H. K. | |
| dc.contributor.author | LAKOMEK, N. A. | |
| dc.contributor.author | HABENSTEIN, Birgit | |
| dc.contributor.author | LOQUET, A. | |
| dc.contributor.author | SHI, C. | |
| dc.contributor.author | GILLER, K. | |
| dc.contributor.author | WOLFF, S. | |
| dc.contributor.author | BECKER, S. | |
| dc.contributor.author | LANGE, A. | |
| dc.date.accessioned | 2020-09-03T08:02:11Z | |
| dc.date.available | 2020-09-03T08:02:11Z | |
| dc.date.issued | 2015 | |
| dc.identifier.issn | 0961-8368 | |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/10983 | |
| dc.description.abstractEn | 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 A 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 beta1-beta2 but also for beta-strands beta1, beta2, beta3 and beta5 as well as for the loop connecting alpha1 and beta3. 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. | |
| dc.language.iso | en | |
| dc.title.en | Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR | |
| dc.title.alternative | Protein science : a publication of the Protein Society | |
| dc.type | Article de revue | |
| dc.identifier.doi | 10.1002/pro.2654 | |
| dc.subject.hal | Chimie/Matériaux | |
| bordeaux.journal | Protein Sci | |
| bordeaux.page | 592-598 | |
| bordeaux.volume | 24 | |
| bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | * |
| bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248) | |
| bordeaux.institution | Université de Bordeaux | |
| bordeaux.institution | Bordeaux INP | |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Protein%20Sci&rft.date=2015&rft.volume=24&rft.spage=592-598&rft.epage=592-598&rft.eissn=0961-8368&rft.issn=0961-8368&rft.au=FASSHUBER,%20H.%20K.&LAKOMEK,%20N.%20A.&HABENSTEIN,%20Birgit&LOQUET,%20A.&SHI,%20C.&rft.genre=article |
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