Protein NMR Resonance Assignment without Spectral Analysis: 5D SOlid-State Automated Projection SpectroscopY (SO-APSY)

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dc.contributor.authorOrton, Henry
dc.contributor.authorStanek, Jan
dc.contributor.authorSchubeis, Tobias
dc.contributor.authorFoucaudeau, Dylan
dc.contributor.authorOllier, Claire
dc.contributor.authorDraney, Adrian W
dc.contributor.authorLe Marchand, Tanguy
dc.contributor.authorCala-De Paepe, Diane
dc.contributor.authorFelli, Isabella C
dc.contributor.authorPierattelli, Roberta
dc.contributor.authorHiller, Sebastian
dc.contributor.authorBermel, Wolfgang
dc.contributor.authorPintacuda, Guido
dc.date.accessioned2021-04-09T00:41:21Z
dc.date.available2021-04-09T00:41:21Z
dc.date.issued2020
dc.description.abstractNarrow proton signals, high sensitivity, and efficient coherence transfers provided by fast magic-angle spinning at high magnetic fields make automated projection spectroscopy feasible for the solid-state NMR analysis of proteins. We present the first ultrahigh dimensional implementation of this approach, where 5D peak lists are reconstructed from a number of 2D projections for protein samples of different molecular sizes and aggregation states, which show limited dispersion of chemical shifts or inhomogeneous broadenings. The resulting datasets are particularly suitable to automated analysis and yield rapid and unbiased assignments of backbone resonances.en_AU
dc.description.sponsorshipThework was funded by the European Research Council(ERC) under the European UnionsHorizon 2020 researchand innovation programme (ERC-2015-CoG GA 648974), bythe CNRS (IR-RMN FR3050), and by the EU-project iNext(GA 653706). H.W.O.was supported by the Westpac Foun-dation with aFuture Leaders Scholarship,and J.S. by the ECsREA with aMSCAfellowship (GA 661799). Theproject wasco-financed by the Polish National Agency for AcademicExchange (contract No PPN/PPO/2018/1/00098)en_AU
dc.format.mimetypeapplication/pdfen_AU
dc.identifier.issn1433-7851en_AU
dc.identifier.urihttp://hdl.handle.net/1885/229740
dc.language.isoen_AUen_AU
dc.provenancehttps://v2.sherpa.ac.uk/id/publication/1320..."The Accepted Version can be archived in a Non-Commercial Institutional Repository. 12 months embargo. " from SHERPA/RoMEO site (as at 9/04/2021). This is the peer reviewed version of the following article: [Orton, Henry W., et al. "Protein NMR Resonance Assignment without Spectral Analysis: 5D SOlid‐State Automated Projection SpectroscopY (SO‐APSY)." Angewandte Chemie International Edition 59.6 (2020): 2380-2384.], which has been published in final form at [https://dx.doi.org/10.1002/anie.201912211]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.en_AU
dc.publisherWileyen_AU
dc.rights© 2019 Wiley-VCH Verlag GmbH &Co. KGaA, Weinheimen_AU
dc.sourceAngewandte Chemieen_AU
dc.subjectnmr spectroscopyen_AU
dc.subjectautomationen_AU
dc.subjectprojection spectroscopyen_AU
dc.subjectproton detectionen_AU
dc.subjectsolid-state structuresen_AU
dc.subjectautomationen_AU
dc.subjectisotope labelingen_AU
dc.subjectnuclear magnetic resonance, biomolecularen_AU
dc.subjectproteinsen_AU
dc.subjectsuperoxide dismutaseen_AU
dc.subjectbeta 2-microglobulinen_AU
dc.titleProtein NMR Resonance Assignment without Spectral Analysis: 5D SOlid-State Automated Projection SpectroscopY (SO-APSY)en_AU
dc.typeJournal articleen_AU
dcterms.accessRightsOpen Accessen_AU
local.bibliographicCitation.issue6en_AU
local.bibliographicCitation.lastpage2384en_AU
local.bibliographicCitation.startpage2380en_AU
local.contributor.affiliationOrton, H., Research School of Chemistry, The Australian National Universityen_AU
local.contributor.authoruidu5376227en_AU
local.identifier.ariespublicationu5786633xPUB1196
local.identifier.citationvolume59en_AU
local.identifier.doi10.1002/anie.201912211en_AU
local.identifier.essn1521-3773en_AU
local.publisher.urlhttps://www.wiley.com/en-gben_AU
local.type.statusAccepted Versionen_AU

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