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首页> 外文期刊>The Journal of Chemical Physics >Accurate measurements of ~(13)C-~(13)C distances in uniformly ~(13)C-labeled proteins using multi-dimensional four-oscillating field solid-state NMR spectroscopy
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Accurate measurements of ~(13)C-~(13)C distances in uniformly ~(13)C-labeled proteins using multi-dimensional four-oscillating field solid-state NMR spectroscopy

机译：使用多维四振荡场固态NMR光谱法精确测量〜（13）C标记的蛋白质中〜（13）C-〜（13）C的距离

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摘要

Application of sets of ~(13)C-~(13)C internuclear distance restraints constitutes a typical key element in determining the structure of peptides and proteins by magic-angle-spinning solid-state NMR spectroscopy. Accurate measurements of the structurally highly important ~(13)C-~(13)C distances in uniformly ~(13)C-labeled peptides and proteins, however, pose a big challenge due to the problem of dipolar truncation. Here, we present novel two-dimensional (2D) solid-state NMR experiments capable of extracting distances between carbonyl (~(13)C') and aliphatic (~(13)C_(aliphatic)) spins with high accuracy. The method is based on an improved version of the four-oscillating field (FOLD) technique [L. A. Straas?, M. Bjerring, N. Khaneja, and N. C. Nielsen, J. Chem. Phys. 130, 225103 (2009)] which circumvents the problem of dipolar truncation, thereby offering a base for accurate extraction of internuclear distances in many-spin systems. The ability to extract reliable accurate distances is demonstrated using one-and two-dimensional variants of the FOLD experiment on uniformly ~(13)C,~(15)N-labeled-L-isoleucine. In a more challenging biological application, FOLD 2D experiments are used to determine a large number of ~(13)C'-~(13)C_(aliphatic) distances in amyloid fibrils formed by the SNNFGAILSS fibrillating core of the human islet amyloid polypeptide with uniform ~(13)C,~(15)N-labeling on the FGAIL fragment.
机译：〜（13）C-〜（13）C核间距离约束集的应用构成了通过魔角旋转固态NMR光谱法确定肽和蛋白质结构的典型关键要素。精确测量〜（13）C标记的肽和蛋白质中〜（13）C-〜（13）C的结构上非常重要的距离，但是由于偶极截短的问题，这带来了很大的挑战。在这里，我们提出了新颖的二维（2D）固态NMR实验，能够准确提取羰基（〜（13）C'）和脂族（〜（13）C_（脂族））自旋之间的距离。该方法基于四振荡场（FOLD）技术的改进版本。 A. Straas？，M。Bjerring，N。Khaneja和N. C. Nielsen，J. Chem。物理130，225103（2009）]规避了偶极截断问题，从而为精确提取多旋系统中的核间距提供了基础。使用FOLD实验的一维和二维变体对〜（13）C，〜（15）N标记的L-异亮氨酸进行均匀的实验，证明了提取可靠准确距离的能力。在更具挑战性的生物学应用中，FOLD 2D实验用于确定人胰岛淀粉样蛋白多肽的SNNFGAILSS纤丝化核心形成的淀粉样蛋白原纤维中的大量〜（13）C'-〜（13）C_（脂族）距离。在FGAIL片段上均匀〜（13）C，〜（15）N标记。

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