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首页> 外文期刊>Journal of Biomolecular NMR >GFT projection NMR spectroscopy for proteins in the solid state
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GFT projection NMR spectroscopy for proteins in the solid state

机译：固态蛋白质的GFT投影NMR光谱

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Recording of four-dimensional (4D) spectra for proteins in the solid state has opened new avenues to obtain virtually complete resonance assignments and three-dimensional (3D) structures of proteins. As in solution state NMR, the sampling of three indirect dimensions leads per se to long minimal measurement time. Furthermore, artifact suppression in solid state NMR relies primarily on radio-frequency pulse phase cycling. For an n-step phase cycle, the minimal measurement times of both 3D and 4D spectra are increased n times. To tackle the associated ‘sampling problem’ and to avoid sampling limited data acquisition, solid state G-Matrix Fourier Transform (SS GFT) projection NMR is introduced to rapidly acquire 3D and 4D spectral information. Specifically, (4,3)D (HA)CANCOCX and (3,2)D (HACA)NCOCX were implemented and recorded for the 6 kDa protein GB1 within about 10% of the time required for acquiring the conventional congeners with the same maximal evolution times and spectral widths in the indirect dimensions. Spectral analysis was complemented by comparative analysis of expected spectral congestion in conventional and GFT NMR experiments, demonstrating that high spectral resolution of the GFT NMR experiments enables one to efficiently obtain nearly complete resonance assignments even for large proteins.
机译：固态蛋白质的四维（4D）光谱记录为获得几乎完整的共振分配和蛋白质的三维（3D）结构开辟了新途径。与在溶液状态NMR中一样，对三个间接维进行采样本身会导致很长的最小测量时间。此外，固态NMR中的伪影抑制主要取决于射频脉冲相位循环。对于n阶相位周期，3D和4D光谱的最小测量时间增加了n倍。为了解决相关的“采样问题”并避免采样限制的数据采集，引入了固态G矩阵傅里叶变换（SS GFT）投影NMR，可以快速采集3D和4D光谱信息。具体而言，在获得具有相同最大最大值的常规同源物所需的时间的大约10％内，对6 kDa蛋白GB1实施并记录了（4,3）D（HA）CANCOCX和（3,2）D（HACA）NCOCX间接尺寸中的演化时间和光谱宽度。在常规和GFT NMR实验中，通过对预期的光谱拥塞进行比较分析，对光谱分析进行了补充，证明了GFT NMR实验的高光谱分辨率使得即使对于大蛋白，也可以有效地获得几乎完整的共振分配。

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