Schanda Paul, Lescop Ewen, Falge Mirjam, Sounier Rémy, Boisbouvier Jérôme, Brutscher Bernhard
Institut de Biologie Structurale - Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, 41, rue Jules Horowitz, 38027, Grenoble Cedex 1, France.
J Biomol NMR. 2007 May;38(1):47-55. doi: 10.1007/s10858-006-9138-2. Epub 2007 Mar 8.
High signal to noise is a necessity for the quantification of NMR spectral parameters to be translated into accurate and precise restraints on protein structure and dynamics. An important source of long-range structural information is obtained from (1)H-(1)H residual dipolar couplings (RDCs) measured for weakly aligned molecules. For sensitivity reasons, such measurements are generally performed on highly deuterated protein samples. Here we show that high sensitivity is also obtained for protonated protein samples if the pulse schemes are optimized in terms of longitudinal relaxation efficiency and J-mismatch compensated coherence transfer. The new sensitivity-optimized quantitative J-correlation experiment yields important signal gains reaching factors of 1.5 to 8 for individual correlation peaks when compared to previously proposed pulse schemes.
高信噪比是将核磁共振光谱参数量化转化为对蛋白质结构和动力学准确且精确的限制条件的必要条件。长程结构信息的一个重要来源是通过对弱取向分子测量的（1）H-（1）H剩余偶极耦合（RDC）获得的。出于灵敏度的原因，此类测量通常在高度氘代的蛋白质样品上进行。在此我们表明，如果在纵向弛豫效率和J失配补偿相干转移方面优化脉冲序列，质子化蛋白质样品也能获得高灵敏度。与先前提出的脉冲序列相比，新的灵敏度优化定量J相关实验使各个相关峰的重要信号增益达到1.5至8倍。
