Nano-mole scale sequential signal assignment by 1 H-detected protein solid-state NMR

Handle URI:
http://hdl.handle.net/10754/594287
Title:
Nano-mole scale sequential signal assignment by 1 H-detected protein solid-state NMR
Authors:
Wang, Songlin; Parthasarathy, Sudhakar; Xiao, Yiling; Nishiyama, Yusuke; Long, Fei; Matsuda, Isamu; Endo, Yuki; Nemoto, Takahiro; Yamauchi, Kazuo; Asakura, Tetsuo; Takeda, Mitsuhiro; Terauchi, Tsutomu; Kainosho, Masatsune; Ishii, Yoshitaka
Abstract:
We 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.
KAUST Department:
Imaging and Characterization Core Lab
Citation:
Wang 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.
Publisher:
Royal Society of Chemistry (RSC)
Journal:
Chem. Commun.
Issue Date:
2015
DOI:
10.1039/c5cc04618a
PubMed ID:
26317132
Type:
Article
ISSN:
1359-7345; 1364-548X
Sponsors:
National Institute of General Medical Sciences[9R01GM098033]; Division of Chemistry[CHE 1310363, CHE 957793]; National Institutes of Health[1S10 RR025105]
Appears in Collections:
Articles; Advanced Nanofabrication, Imaging and Characterization Core Lab

Full metadata record

DC FieldValue Language
dc.contributor.authorWang, Songlinen
dc.contributor.authorParthasarathy, Sudhakaren
dc.contributor.authorXiao, Yilingen
dc.contributor.authorNishiyama, Yusukeen
dc.contributor.authorLong, Feien
dc.contributor.authorMatsuda, Isamuen
dc.contributor.authorEndo, Yukien
dc.contributor.authorNemoto, Takahiroen
dc.contributor.authorYamauchi, Kazuoen
dc.contributor.authorAsakura, Tetsuoen
dc.contributor.authorTakeda, Mitsuhiroen
dc.contributor.authorTerauchi, Tsutomuen
dc.contributor.authorKainosho, Masatsuneen
dc.contributor.authorIshii, Yoshitakaen
dc.date.accessioned2016-01-19T14:45:15Zen
dc.date.available2016-01-19T14:45:15Zen
dc.date.issued2015en
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.en
dc.identifier.issn1359-7345en
dc.identifier.issn1364-548Xen
dc.identifier.pmid26317132en
dc.identifier.doi10.1039/c5cc04618aen
dc.identifier.urihttp://hdl.handle.net/10754/594287en
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.en
dc.description.sponsorshipNational Institute of General Medical Sciences[9R01GM098033]en
dc.description.sponsorshipDivision of Chemistry[CHE 1310363, CHE 957793]en
dc.description.sponsorshipNational Institutes of Health[1S10 RR025105]en
dc.publisherRoyal Society of Chemistry (RSC)en
dc.titleNano-mole scale sequential signal assignment by 1 H-detected protein solid-state NMRen
dc.typeArticleen
dc.contributor.departmentImaging and Characterization Core Laben
dc.identifier.journalChem. Commun.en
dc.contributor.institutionDepartment of Chemistry, University of Illinois at Chicago, Chicago, IL, United Statesen
dc.contributor.institutionJEOL RESONANCE Inc., 3-1-2 Musashino, Akishima, Tokyo, Japanen
dc.contributor.institutionRIKEN, CLST-JEOL Collaboration Center, Yokohama, Kanagawa, Japanen
dc.contributor.institutionSchool of Science and Technology, Nazarbayev University, Astana, Kazakhstanen
dc.contributor.institutionDepartment of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo, Japanen
dc.contributor.institutionStructure Biology Research Center, Graduate School of Science, Nagoya University, Furocho, Chikusa-ku, Nagoya, Japanen
dc.contributor.institutionSAIL Technologies Inc., 2008-2 Wada, Tama, Tokyo, Japanen
dc.contributor.institutionGraduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minami-ohsawa, Hachioji, Tokyo, Japanen
dc.contributor.institutionCenter for Structural Biology, University of Illinois at Chicago, Chicago, IL, United Statesen
kaust.authorYamauchi, Kazuoen

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