Nano-mole scale sequential signal assignment by 1 H-detected protein solid-state NMR
KAUST DepartmentImaging and Characterization Core Lab
Embargo End Date2016-08-28
Permanent link to this recordhttp://hdl.handle.net/10754/594287
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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.
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.
SponsorsNational Institute of General Medical Sciences[9R01GM098033]
Division of Chemistry[CHE 1310363, CHE 957793]
National Institutes of Health[1S10 RR025105]
PublisherRoyal Society of Chemistry (RSC)
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