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首页> 外文期刊>Journal of magnetic resonance >Determination of Polypeptide Backbone Dihedral Angles in Solid State NMR by Double Quantum ~(13)C Chemical Shift Anisotropy Measurements
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Determination of Polypeptide Backbone Dihedral Angles in Solid State NMR by Double Quantum ~(13)C Chemical Shift Anisotropy Measurements

机译：双量子〜（13）C化学位移各向异性测量法测定固态NMR中的多肽骨架二面角

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摘要

A solid state NMR technique for the determination of peptide backbone conformations at specific sites in unoriented samples under magic angle spinning (MAS) is described and demonstrated on a doubly labeled polycrystalline sample of the tripeptide AlaGlyGly and a sextuply labeled lyophilized sample of the 17-residue peptide MB(i + 4)EK. The technique is applicable to peptides and proteins that are labeled with ~(13)C at two (or more) consecutive backbone carbonyl sites. Double quantum (DQ) coherences are excited wit a radiofrequency-driven recoupling sequence and evolve during a constant-time t_1 period at the sum of the two anisotropic chemical shifts. The relative orientation of the two chemical shift anisotropy (CSA) tensors, which depends on the φ and ψ backbone dihedral angles, determines the t_1-dependence of spinning sideband intensities in the DQ-filtered ~(13)C MAS spectrum. Experiments and simulations show that both dihedral angles can be extracted from a single data set. This technique, called DQCSA spectroscopy, may be especially useful when analyzing the backbone conformation of a polypeptide at a particular doubly labeled site in the presence of additional labeled carbons along the sequence.
机译：描述了一种固态NMR技术，该方法用于在幻角旋转（MAS）下测定未取向样品中特定位点的肽骨架构象，并在三肽AlaGlyGly的双标记多晶样品和17残基的六重标记冻干样品上进行了证明。肽MB（i + 4）EK。该技术适用于在两个（或多个）连续的主链羰基位点被〜（13）C标记的肽和蛋白质。双量子（DQ）相干通过射频驱动的重新耦合序列被激发，并在两个各向异性化学位移之和的恒定时间t_1周期内演化。两个化学位移各向异性（CSA）张量的相对方向取决于φ和ψ主干二面角，它决定了DQ滤波后的〜（13）C MAS光谱中纺丝边带强度的t_1依赖性。实验和仿真表明，可以从单个数据集中提取两个二面角。在沿序列存在其他标记碳的情况下，分析特定双标记位点处多肽的骨架构象时，这种称为DQCSA光谱学的技术可能特别有用。

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