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首页> 外文期刊>Journal of magnetic resonance >Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments
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Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments

机译：通过基于TROSY的J调制实验测量大蛋白中的一键和二键N-C偶联

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摘要

Residual dipolar couplings (RDCs) between NC' and NC alpha atoms in polypeptide backbones of proteins contain information on the orientation of bond vectors that is complementary to that contained in NH RDCs. The (1)J(NC alpha) and (2)J(NC alpha) scalar couplings between these atoms also display a Karplus relation with the backbone torsion angles and report on secondary structure. However, these N-C couplings tend to be small and they are frequently unresolvable in frequency domain spectra having the broad lines characteristic of large proteins. Here a TROSY-based J-modulated approach for the measurement of small N-15-C-13 couplings in large proteins is described. The cross-correlation interference effects inherent in TROSY methods improve resolution and signal to noise ratios for large proteins, and the use of J-modulation to encode couplings eliminates the need to remove frequency distortions from overlapping peaks during data analysis. The utility of the method is demonstrated by measurement of (1)J(NC'), (1)J(NC alpha), and (2)J(NC alpha) scalar couplings and D-1(NC') and D-1(NC alpha) residual dipolar couplings for the myristoylated yeast ARF1 GTP gamma s protein bound to small lipid bicelles, a system with an effective molecule weight of similar to 70 kDa.
机译：蛋白质多肽主链中NC'和NCα原子之间的残留偶极偶合（RDC）包含有关键载体方向的信息，该信息与NH RDC中所包含的互补。这些原子之间的（1）J（NC alpha）和（2）J（NC alpha）标量耦合也显示与骨架扭转角的Karplus关系，并报告二级结构。但是，这些N-C偶合往往很小，并且在具有大蛋白特征的宽谱线的频域谱中经常无法分辨。这里介绍了一种基于TROSY的J调制方法，用于测量大蛋白中的小N-15-C-13偶联。 TROSY方法固有的互相关干扰效应可提高大蛋白的分辨率和信噪比，并且使用J调制来编码偶联消除了在数据分析过程中消除重叠峰的频率失真的需要。该方法的实用性通过测量（1）J（NC'），（1）J（NC alpha）和（2）J（NC alpha）标量耦合以及D-1（NC'）和D-肉豆蔻酰化的酵母ARF1 GTPγs蛋白的1（NCα）残留偶极偶合与小脂质双胞胎结合的系统，其有效分子量类似于70 kDa。

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