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dc.contributor.authorSTANEK, Jan
dc.contributor.authorANDREAS, Loren B.
dc.contributor.authorJAUDZEMS, Kristaps
dc.contributor.authorCALA, Diane
dc.contributor.authorLALLI, Daniela
dc.contributor.authorBERTARELLO, Andrea
dc.contributor.authorSCHUBEIS, Tobias
dc.contributor.authorAKOPJANA, Inara
dc.contributor.authorKOTELOVICA, Svetlana
dc.contributor.authorTARS, Kaspars
dc.contributor.authorPICA, Andrea
dc.contributor.authorLEONE, Serena
dc.contributor.authorPICONE, Delia
dc.contributor.authorXU, Zhi-Qiang
dc.contributor.authorDIXON, Nicholas E.
dc.contributor.authorMARTINEZ, Denis
dc.contributor.authorBERBON, Melanie
dc.contributor.authorEL MAMMERI, Nadia
dc.contributor.authorNOUBHANI, Abdelmajid
dc.contributor.authorSAUPE, Sven
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorPINTACUDA, Guido
dc.date.accessioned2020-09-03T07:56:06Z
dc.date.available2020-09-03T07:56:06Z
dc.date.issued2016
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10821
dc.description.abstractEnWe demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR spectroscopy with 100-111 kHz magic-angle spinning (MAS). The excellent resolution in the Calpha-Halpha plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Calpha-Halpha detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 mug of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.
dc.language.isoen
dc.title.enNMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils
dc.typeArticle de revue
dc.identifier.doi10.1002/anie.201607084
dc.subject.halChimie/Matériaux
bordeaux.journalAngewandte Chemie (International ed. in English)
bordeaux.page15503-15509
bordeaux.volume55
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.issue50
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Angewandte%20Chemie%20(International%20ed.%20in%20English)&rft.date=2016&rft.volume=55&rft.issue=50&rft.spage=15503-15509&rft.epage=15503-15509&rft.au=STANEK,%20Jan&ANDREAS,%20Loren%20B.&JAUDZEMS,%20Kristaps&CALA,%20Diane&LALLI,%20Daniela&rft.genre=article


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