Dual-band selective double cross polarization for heteronuclear polarization transfer between dilute spins in solid-state MAS NMR.
Dual-band selective double cross polarization for heteronuclear polarization transfer between dilute spins in solid-state MAS NMR.
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DOI：
10.1016/j.jmr.2012.02.020
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发表时间：
2012-04
期刊：
影响因子：
--
通讯作者：
Fu R
中科院分区：
文献类型：
--
作者：
Zhang Z;Miao Y;Liu X;Yang J;Li C;Deng F;Fu R
本文描述了双交叉极化魔角旋转核磁共振谱中两个稀自旋之间选择性异质极化转移的正弦调制方案。在第二次N → C交叉极化期间，13C RF幅度被正弦调制，而15N RF幅度是正切的。该调制在13C RF载波频率的任一侧中的两个选择性频带中诱导有效的自旋锁定场，从而允许在这两个选择性频带中从15N到13C的同时极化转移。实验和模拟结果表明，这种正弦调制可以同时选择性地从15 N到相邻肽平面上共价键合的13 C α和13 C ′碳，这对于在蛋白质结构解析中建立两个连续残基之间的骨架连接是有用的。实验证明了13 C，15 N标记的G蛋白β1免疫球蛋白结合域（GB1）的选择性和有效性。
A sinusoidal modulation scheme is described for selective heteronuclear polarization transfer between two dilute spins in double cross polarization magic-angle-spinning nuclear magnetic resonance spectroscopy. During the second N → C cross polarization, the 13C RF amplitude is modulated sinusoidally while the 15N RF amplitude is tangent. This modulation induces an effective spin-lock field in two selective frequency bands in either side of the 13C RF carrier frequency, allowing for simultaneous polarization transfers from 15N to 13C in those two selective frequency bands. It is shown by experiments and simulations that this sinusoidal modulation allows one to selectively polarize from 15N to its covalently bonded 13Cα and 13C′ carbons in neighboring peptide planes simultaneously, which is useful for establishing the back-bone connectivity between two sequential residues in protein structural elucidation. The selectivity and efficiency were experimentally demonstrated on a uniformly 13C,15N-labeled β1 immunoglobulin binding domain of protein G (GB1).
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影响因子：
15
作者：
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