通过氢检测的蛋白质固态核磁共振进行纳摩尔级别的序列信号归属。
Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.
作者信息
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
机构信息
Department of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA.
出版信息
Chem Commun (Camb). 2015 Oct 18;51(81):15055-8. doi: 10.1039/c5cc04618a. Epub 2015 Aug 28.
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.
摘要
我们提出了一种3D（1）H检测的固态核磁共振（SSNMR）方法，用于使用约80 kHz的超快魔角旋转（MAS），通过一种新颖的光谱编辑方法对10 - 100 nmol的完全质子化蛋白质进行主链信号分配，该方法可实现显著的光谱简化。与传统的3D（13）C检测的SSNMR方法相比，该方法节省了约110倍的时间。
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