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首页> 外文期刊>Journal of the American Chemical Society >A Multidimensional NMR Experiment for Measurement of the Protein Dihedral Angle ψ Based on Cross-Correlated Relaxation between ~1H~α -~13C~α Dipolar and ~13C' (Carbonyl) Chemical Shift Anisotropy Mechanisms
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A Multidimensional NMR Experiment for Measurement of the Protein Dihedral Angle ψ Based on Cross-Correlated Relaxation between ~1H~α -~13C~α Dipolar and ~13C' (Carbonyl) Chemical Shift Anisotropy Mechanisms

机译：基于〜1H〜α-〜13C〜α偶极与〜13C'（羰基）化学位移各向异性机制之间互相关弛豫的多维NMR实验，用于测量蛋白质二面角ψ

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摘要

A high-resolution triple-resonance NMR method is presented for the measurement of the backbone dihedral angle ψ based on cross-correlated relaxation between ~1H~α-~13C~α dipolar and ~13C' (carbonyl) chemical shift anisortropy relaxation mechanisms. The method relies on measurement of peak intensities of multiplet components is spectra recording zero-and double-quantum ~13C~α-~13C' coherences. Resultsbased on two proteins, ubiquitin and CheY, demonstrate a well-defined relation between cross-correlation rate and ψ. Shift Anisotropy Mechanisms
机译：基于〜1H〜α-〜13C〜α偶极子与〜13C'（羰基）化学位移各向异性弛豫机制之间的互相关弛豫，提出了一种高分辨率的三共振核磁共振方法，用于测量骨架二面角ψ。该方法依赖于测量多重峰成分的峰值强度，即记录零和双量子〜13C〜α-〜13C'相干的光谱。基于两种蛋白质，泛素和CheY的结果证明了互相关率和ψ之间的关系明确。位移各向异性机制

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