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Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR

dc.contributor.authorFASSHUBER, H. K.
dc.contributor.authorLAKOMEK, N. A.
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorLOQUET, A.
dc.contributor.authorSHI, C.
dc.contributor.authorGILLER, K.
dc.contributor.authorWOLFF, S.
dc.contributor.authorBECKER, S.
dc.contributor.authorLANGE, A.
dc.date.accessioned2020-09-03T08:02:11Z
dc.date.available2020-09-03T08:02:11Z
dc.date.issued2015
dc.identifier.issn0961-8368
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10983
dc.description.abstractEnBy 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.isoen
dc.title.enStructural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR
dc.title.alternativeProtein science : a publication of the Protein Society
dc.typeArticle de revue
dc.identifier.doi10.1002/pro.2654
dc.subject.halChimie/Matériaux
bordeaux.journalProtein Sci
bordeaux.page592-598
bordeaux.volume24
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_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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