用于13C-15N双标记蛋白质中多肽主链归属的3D 13C-15N异核双自旋相干光谱法。
3D 13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double-labeled proteins.
作者信息
Szyperski T, Wider G, Bushweller J H, Wüthrich K
机构信息
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
出版信息
J Biomol NMR. 1993 Jan;3(1):127-32. doi: 10.1007/BF00242481.
The pulse sequence of a new constant-time 3D triple-resonance experiment, ct-HA[CAN]HN, is presented. This experiment delineates exclusively scalar connectivities and uses 13C alpha-15N heteronuclear two-spin coherence to overlay the chemical shift evolution periods of the 13C alpha and 15N nuclei, thereby providing the four resonance frequencies of the alpha-proton, the alpha-carbon, the amide nitrogen, and the amide proton of a given amino acid residue in three dimensions. This experiment promises to be a valid alternative to 4D experiments, providing the same information on intraresidue polypeptide backbone connectivities in 13C-15N-double-labeled proteins.
本文介绍了一种新的恒定时间3D三共振实验ct-HA[CAN]HN的脉冲序列。该实验专门描绘标量连接性，并利用13Cα-15N异核双自旋相干来叠加13Cα和15N核的化学位移演化期，从而在三维空间中提供给定氨基酸残基的α-质子、α-碳、酰胺氮和酰胺质子的四个共振频率。该实验有望成为4D实验的有效替代方法，在13C-15N双标记蛋白质中提供关于残基内多肽主链连接性的相同信息。
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