Backbone assignment of fully protonated solid proteins by 1 H detection and ultrafast magic-angle-spinning NMR spectroscopy

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dc.contributor.authorMarchetti, Alessandro
dc.contributor.authorJehle, Stefan
dc.contributor.authorFelletti, Michele
dc.contributor.authorKnight, Michael J.
dc.contributor.authorWang, Yao
dc.contributor.authorXu, Zhi-Qiang
dc.contributor.authorPark, Ah Young
dc.contributor.authorLesage, Anne
dc.contributor.authorEmsley, Lyndon
dc.contributor.authorDixon, Nicholas Edward
dc.contributor.authorPintacuda, Guido
dc.contributor.authorOtting, Gottfried
dc.date.accessioned2015-12-07T22:30:42Z
dc.date.issued2012
dc.date.updated2016-02-24T11:39:27Z
dc.description.abstractNarrow 1H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic-angle spinning (60 kHz). Medium-size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone 1H, 15N, 13C α, and 13CO resonances and yields information about 1H-1H proximities.
dc.identifier.issn1433-7851
dc.identifier.urihttp://hdl.handle.net/1885/22428
dc.publisherWiley-VCH Verlag GMBH
dc.sourceAngewandte Chemie International Edition
dc.subjectKeywords: Deuterations; DNA polymerase; Magic-angle-spinning NMR; Noncrystalline proteins; Protein samples; Protein structures; Protonated; scalar transfers; Solid protein; Ultra-fast; Deuterium; Nuclear magnetic resonance spectroscopy; Proteins; Protonation; Magic DNA polymerase; magic-angle spinning; NMR spectroscopy; protein structures; scalar transfers
dc.titleBackbone assignment of fully protonated solid proteins by 1 H detection and ultrafast magic-angle-spinning NMR spectroscopy
dc.typeJournal article
local.bibliographicCitation.issue43
local.bibliographicCitation.lastpage10759
local.bibliographicCitation.startpage10756
local.contributor.affiliationMarchetti, Alessandro, University of Lyon
local.contributor.affiliationJehle, Stefan, University of Lyon
local.contributor.affiliationFelletti, Michele, University of Lyon
local.contributor.affiliationKnight, Michael J., University of Lyon
local.contributor.affiliationWang, Yao, University of Wollongong
local.contributor.affiliationXu, Zhi-Qiang, University of Wollongong
local.contributor.affiliationPark, Ah Young, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationOtting, Gottfried, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationLesage, Anne, University of Lyon
local.contributor.affiliationEmsley, Lyndon, University of Lyon
local.contributor.affiliationDixon, Nicholas Edward, University of Wollongong
local.contributor.affiliationPintacuda, Guido, Ecole Normale Superieure de Lyon
local.contributor.authoruidPark, Ah Young, u4015196
local.contributor.authoruidOtting, Gottfried, u4046684
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030403 - Characterisation of Biological Macromolecules
local.identifier.absseo970106 - Expanding Knowledge in the Biological Sciences
local.identifier.ariespublicationu8302325xPUB21
local.identifier.ariespublicationU4217927xPUB818
local.identifier.citationvolume51
local.identifier.doi10.1002/anie.201203124
local.identifier.scopusID2-s2.0-84867548984
local.identifier.thomsonID000310076100012
local.type.statusPublished Version

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