A study was conducted to demonstrate the use of NMR as a as a tool to determine the structures, folding behavior, dynamics, and interactions of plant proteins. Investigations revealed that one-dimensional (1D) spectra were useful for rapid characterization of the folding or structure of smaller proteins. Correct folding was associated with sharp spectral lines and good dispersion of the amide signals or the observation of some upfield-shifted methyl groups. Upfield or down field dispersion of the α-H shifts provided a measure of helical or β-sheet secondary structure. A quick measure of the folding of proteins was also obtained from the pattern of chemical shifts in two-dimensional (2D) HSQC spectra for larger proteins. This was conveniently done with N-labeled samples, but the sensitivity of modern instruments equipped with cryo-probes allowed 2D HSQC spectra to be recorded for natural abundance samples.

中文翻译：

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植物蛋白的核磁共振

进行了一项研究以证明使用 NMR 作为确定植物蛋白质结构、折叠行为、动力学和相互作用的工具。研究表明，一维 (1D) 光谱可用于快速表征较小蛋白质的折叠或结构。正确折叠与清晰的谱线和酰胺信号的良好分散或观察到一些上场位移的甲基有关。α-H 位移的上场或下场分散提供了螺旋或 β-折叠二级结构的测量。蛋白质折叠的快速测量也可从较大蛋白质的二维 (2D) HSQC 光谱中的化学位移模式中获得。这可以方便地用 N 标记的样本完成，