一种用于确定蛋白质侧链1H和13C共振峰归属的4D HCCH-TOCSY实验。
A 4D HCCH-TOCSY experiment for assigning the side chain 1H and 13C resonances of proteins.
作者信息
Olejniczak E T, Xu R X, Fesik S W
机构信息
Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064.
出版信息
J Biomol NMR. 1992 Nov;2(6):655-9. doi: 10.1007/BF02192854.
A 4D HCCH-TOCSY experiment is described for correlating and assigning the 1H and 13C resonances of protein amino acid side chains that has several advantages over 3D versions of the experiment. In many cases, both the 1H and 13C chemical shifts can be obtained in the 4D experiment from a simple inspection of the 13C(omega 3), 1H(omega 4) planes extracted at the 1H alpha(omega 1)/13C alpha(omega 2) chemical shifts. Together with the 3D and 4D triple resonance experiments, this allows sequence-specific assignments to be obtained. In addition, the increased resolution of the 4D experiment compared to its 3D counterpart allows automation of resonance assignments.
本文描述了一种用于关联和指认蛋白质氨基酸侧链的¹H和¹³C共振的4D HCCH-TOCSY实验，该实验相对于3D版本的实验具有多个优势。在许多情况下，通过简单检查在¹Hα(ω1)/¹³Cα(ω2)化学位移处提取的¹³C(ω3)、¹H(ω4)平面，就可以在4D实验中获得¹H和¹³C化学位移。结合3D和4D三重共振实验，这使得能够获得序列特异性指认。此外，与3D实验相比，4D实验分辨率的提高使得共振指认能够自动化。
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