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

ABSTRACT: We present a 3D (1)H-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 (13)C-detected SSNMR approach.

SUBMITTER: Wang S

PROVIDER: S-EPMC4589527 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature

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

Wang Songlin S Parthasarathy Sudhakar S Xiao Yiling Y Nishiyama Yusuke Y Long Fei F Matsuda Isamu I Endo Yuki Y Nemoto Takahiro T Yamauchi Kazuo K Asakura Tetsuo T Takeda Mitsuhiro M Terauchi Tsutomu T Kainosho Masatsune M Ishii Yoshitaka Y

Chemical communications (Cambridge, England) 20150828 81

We present a 3D (1)H-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 (13)C-detected SSNMR approach. ...[more]

PMID: 26317132

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