降低的构象（4，3）D-hnCOCANH实验：蛋白质NMR研究的有效骨架分配工具
Reduced Dimensionality (4,3)D-hnCOCANH Experiment: An Efficient Backbone Assignment tool for NMR studies of Proteins
摘要：
序列特异性共振归属和蛋白质的二级结构测定构成了利用NMR进行各种结构和功能蛋白质组学研究的基础。在这种情况下，一个有效的独立的方法快速分配的骨干（1H，15 N，13 Ca和13 C '）的共振和二级结构的测定蛋白质已在这里提出。与目前用于该目的的可用策略相比，该方法仅采用单一的降维（RD）实验-（4，3）D-hnCOCANH，并利用骨架（13 Ca和13 C '）化学位移的线性组合来实现与单个化学位移（参见正文）相比相对更好的分散，以进行有效和快速的数据分析。此外，该实验导致具有自身（残基内）和连续（残基间）碳相关峰的直接区别的光谱;这些峰在符号上相反，因此可以容易地区分，而无需使用额外的补充实验。最重要的是，该方法的主要优势在于其基于以下内容的高效且鲁棒的分配策略：（a）多个，（b）在不同的[（F_1（13 C）-F_3（1H）]和[（F_2（15 N）-F_3（1H）]]中，3D光谱的平面，其使得能够容易地识别某些特定的三重序列（参见文本），并且因此用作用于将顺序连接的HSQC交叉峰的延伸映射到主要序列上的检查点，用于具体地分配共振序列。总体而言，这里提出的独立方法将是一个重要的骨干分配工具的结构和功能蛋白质组学，蛋白质折叠，和药物发现的NMR研究计划。
英文摘要：
Sequence specific resonance assignment and secondary structure determination of proteins form the basis for variety of structural and functional proteomics studies by NMR. In this context, an efficient standalone method for rapid assignment of backbone (1H, 15N, 13Ca and 13C') resonances and secondary structure determination of proteins has been presented here. Compared to currently available strategies used for the purpose, the method employs only a single reduced dimensionality (RD) experiment -(4,3)D-hnCOCANH and exploits the linear combinations of backbone (13Ca and 13C') chemical shifts to achieve a dispersion relatively better compared to those of individual chemical shifts (see the text) for efficient and rapid data analysis. Further, the experiment leads to the spectrum with direct distinction of self (intra-residue) and sequential (inter-residue) carbon correlation peaks; these appear opposite in signs and therefore can easily be discriminated without using an additional complementary experiment. On top of all this, the main strength of the method is its efficient and robust assignment strategy based on: (a) multiple, but unidirectional sequential 15N and 13C correlations (i-->i-1) and (b) the distinctive peak patterns of self and sequential peaks in different [(F1(13C)-F3(1H) and (F2(15N)-F3(1H)] planes of the 3D spectrum which enable ready identification of certain specific triplet sequences (see the text) and thus serve as check points for mapping the stretches of sequentially connected HSQC cross peaks on to the primary sequence for assigning the resonances sequence specifically. Overall, the standalone method presented here will be an important backbone assignment tool for structural and functional proteomics, protein folding, and drug discovery research programs by NMR.
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