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dc.contributor.authorWang, Songlin
dc.contributor.authorParthasarathy, Sudhakar
dc.contributor.authorXiao, Yiling
dc.contributor.authorNishiyama, Yusuke
dc.contributor.authorLong, Fei
dc.contributor.authorMatsuda, Isamu
dc.contributor.authorEndo, Yuki
dc.contributor.authorNemoto, Takahiro
dc.contributor.authorYamauchi, Kazuo
dc.contributor.authorAsakura, Tetsuo
dc.contributor.authorTakeda, Mitsuhiro
dc.contributor.authorTerauchi, Tsutomu
dc.contributor.authorKainosho, Masatsune
dc.contributor.authorIshii, Yoshitaka
dc.date.accessioned2016-01-19T14:45:15Z
dc.date.available2016-01-19T14:45:15Z
dc.date.issued2015-08-28
dc.identifier.citationWang S, Parthasarathy S, Xiao Y, Nishiyama Y, Long F, et al. (2015) Nano-mole scale sequential signal assignment by 1 H-detected protein solid-state NMR . Chem Commun 51: 15055–15058. Available: http://dx.doi.org/10.1039/c5cc04618a.
dc.identifier.issn1359-7345
dc.identifier.issn1364-548X
dc.identifier.pmid26317132
dc.identifier.doi10.1039/c5cc04618a
dc.identifier.urihttp://hdl.handle.net/10754/594287
dc.description.abstractWe present a 3D 1H-detected solid-state NMR (SSNMR) approach for main-chain signal assignments of 10-100 nmol of fully protonated proteins using ultra-fast magic-angle spinning (MAS) at ∼80 kHz by a novel spectral-editing method, which permits drastic spectral simplification. The approach offers ∼110 fold time saving over a traditional 3D 13C-detected SSNMR approach. This journal is © The Royal Society of Chemistry 2015.
dc.description.sponsorshipNational Institute of General Medical Sciences[9R01GM098033]
dc.description.sponsorshipDivision of Chemistry[CHE 1310363, CHE 957793]
dc.description.sponsorshipNational Institutes of Health[1S10 RR025105]
dc.publisherRoyal Society of Chemistry (RSC)
dc.relation.urlhttp://europepmc.org/articles/pmc4589527?pdf=render
dc.rightsArchived with thanks to Royal Society of Chemistry (RSC)
dc.rightsThis file is an open access version redistributed from: http://europepmc.org/articles/pmc4589527?pdf=render
dc.titleNano-mole scale sequential signal assignment by 1 H-detected protein solid-state NMR
dc.typeArticle
dc.contributor.departmentImaging and Characterization Core Lab
dc.identifier.journalChem. Commun.
dc.rights.embargodate2016-08-28
dc.eprint.versionPost-print
dc.contributor.institutionDepartment of Chemistry, University of Illinois at Chicago, Chicago, IL, United States
dc.contributor.institutionJEOL RESONANCE Inc., 3-1-2 Musashino, Akishima, Tokyo, Japan
dc.contributor.institutionRIKEN, CLST-JEOL Collaboration Center, Yokohama, Kanagawa, Japan
dc.contributor.institutionSchool of Science and Technology, Nazarbayev University, Astana, Kazakhstan
dc.contributor.institutionDepartment of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo, Japan
dc.contributor.institutionStructure Biology Research Center, Graduate School of Science, Nagoya University, Furocho, Chikusa-ku, Nagoya, Japan
dc.contributor.institutionSAIL Technologies Inc., 2008-2 Wada, Tama, Tokyo, Japan
dc.contributor.institutionGraduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minami-ohsawa, Hachioji, Tokyo, Japan
dc.contributor.institutionCenter for Structural Biology, University of Illinois at Chicago, Chicago, IL, United States
kaust.personYamauchi, Kazuo
refterms.dateFOA2020-06-30T12:58:17Z


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