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dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLENDS, Alons
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERBON, Melanie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorNISHIYAMA, Yusuke
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
dc.date.accessioned2024-04-16T13:41:34Z
dc.date.available2024-04-16T13:41:34Z
dc.date.issued2021-12-01
dc.identifier.issn1573-5001en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199112
dc.description.abstractEnSolid-state NMR spectroscopy is a powerful technique to study insoluble and non-crystalline proteins and protein complexes at atomic resolution. The development of proton (1H) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of 1H-detected fingerprint experiments in few hours. Here an approach based on double-quantum (DQ) 13C spectroscopy, detected on 1H, is proposed for fast MAS regime (> 60 kHz) to perform the sequential assignment of insoluble proteins of small size, without any specific deuteration requirement. By combining two three-dimensional 1H detected experiments correlating a 13C DQ dimension respectively to its intra-residue and sequential 15 N-1H pairs, a sequential walk through DQ (Ca + CO) resonance is obtained. The approach takes advantage of fast MAS to achieve an efficient sensitivity and the addition of a DQ dimension provides spectral features useful for the resonance assignment process.
dc.language.isoENen_US
dc.subject.enFast MAS
dc.subject.enProtein NMR
dc.subject.enProton detection
dc.subject.enSolid-State NMR
dc.title.enProtein resonance assignment by solid-state NMR based on 1H-detected 13C double-quantum spectroscopy at fast MAS
dc.title.alternativeJ Biomol NMRen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1007/s10858-021-00386-6en_US
dc.subject.halChimie/Matériauxen_US
dc.identifier.pubmed34813018en_US
bordeaux.journalJournal of biomolecular NMRen_US
bordeaux.page417-427en_US
bordeaux.volume75en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue10en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal%20of%20biomolecular%20NMR&rft.date=2021-12-01&rft.volume=75&rft.issue=10&rft.spage=417-427&rft.epage=417-427&rft.eissn=1573-5001&rft.issn=1573-5001&rft.au=LENDS,%20Alons&BERBON,%20Melanie&HABENSTEIN,%20Birgit&NISHIYAMA,%20Yusuke&LOQUET,%20Antoine&rft.genre=article


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