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

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dc.abstract.enNarrow 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 utomated analysis and yield rapid and unbiased assignments of backbone resonances.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorStanek, Jan
dc.contributor.authorDraney, Adrian W.
dc.contributor.authorFoucaudeau, Dylan
dc.contributor.authorSchubeis, Tobias
dc.contributor.authorOllier, Claire
dc.contributor.authorOrton, Henry W.
dc.contributor.authorBermel, Wolfgang
dc.contributor.authorHiller, Sebastian
dc.contributor.authorPintacuda, Guido
dc.contributor.authorPaepe, Diane Cala-De
dc.contributor.authorMarchand, Tanguy Le
dc.contributor.authorPierattelli, Roberta
dc.contributor.authorFelli, Isabella C.
dc.date.accessioned2024-01-25T18:20:53Z
dc.date.available2024-01-25T18:20:53Z
dc.date.issued2020
dc.description.financePublikacja bezkosztowa
dc.description.number6
dc.description.volume59
dc.identifier.doi10.1002/ANIE.201912211
dc.identifier.issn1433-7851
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/117309
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofAngewandte Chemie - International Edition
dc.relation.pages2380-2384
dc.rightsClosedAccess
dc.sciencecloudnosend
dc.titleProtein NMR Resonance Assignment without Spectral Analysis: 5D SOlid-State Automated Projection SpectroscopY (SO-APSY)
dc.typeJournalArticle
dspace.entity.typePublication