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在单个三维谱中对五个频率进行高分辨率检测:HNHCACO——一种双向相干转移实验。

High-resolution detection of five frequencies in a single 3D spectrum: HNHCACO--a bidirectional coherence transfer experiment.

作者信息

Pang Y, Zeng L, Kurochkin A V, Zuiderweg E R

机构信息

Biophysics Research Division, University of Michigan, Ann Arbor 48109-1055, USA.

出版信息

J Biomol NMR. 1998 Feb;11(2):185-90. doi: 10.1023/a:1008229723544.

DOI:10.1023/a:1008229723544
PMID:9679293
Abstract

A new triple-resonance pulse sequence, 3D HNHCACO, is introduced and discussed, which identifies sequential correlations of the backbone nuclei (H alpha (i-1), C alpha (i-1), C(i-1), NH(i), N(i)) of doubly labeled proteins in H2O. The three-dimensional (3D) method utilizes a recording of 15N and 13C resonances in a single indirect time domain, the 13C' resonance in another indirect time domain, and detects both NH and H alpha protons. A bidirectional coherence transfer (NH(i) <--> N(i) <--> C(i-1) <--> C alpha (i-1) <--> H alpha (i-1)) is effectuated, resulting in a single high-resolution 3D spectrum that contains the frequencies of all five backbone nuclei. The experiment was applied to the 12.3 kDa ribonuclease from Bacillus intermedius (Binase).

摘要

本文介绍并讨论了一种新的三共振脉冲序列——3D HNHCACO,该序列可识别H2O中双标记蛋白质主链核(Hα(i - 1)、Cα(i - 1)、C(i - 1)、NH(i)、N(i))的顺序相关性。这种三维(3D)方法在单个间接时域中记录15N和13C共振,在另一个间接时域中记录13C′共振,并同时检测NH和Hα质子。实现了双向相干转移(NH(i) <--> N(i) <--> C(i - 1) <--> Cα(i - 1) <--> Hα(i - 1)),从而得到一个包含所有五个主链核频率的单一高分辨率3D谱。该实验应用于来自中间芽孢杆菌的12.3 kDa核糖核酸酶(Binase)。

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本文引用的文献

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J Biomol NMR. 1995 Feb;5(2):202-6. doi: 10.1007/BF00208811.
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A simultaneous (15)N, (1)H- and (13)C, (1)H-HSQC with sensitivity enhancement and a heteronuclear gradient echo.带灵敏度增强的 (15)N、(1)H- 和 (13)C、(1)H-HSQC 及异核梯度回波的同时检测。
J Biomol NMR. 1995 Jan;5(1):97-102. doi: 10.1007/BF00227475.
3
Time-saving methods for heteronuclear multidimensional NMR of ((13)C, (15)N) doubly labeled proteins.
((13)C, (15)N)双标记蛋白质的异核多维 NMR 的省时方法。
J Biomol NMR. 1994 Mar;4(2):201-13. doi: 10.1007/BF00175248.
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A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins.一种新的三重共振实验,用于蛋白质中骨架共振的顺序赋值。
J Biomol NMR. 1995 Sep;6(2):189-97. doi: 10.1007/BF00211783.
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Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.在均匀13C/15N标记蛋白质的序列归属过程中氨基酸类型的确定。
J Biomol NMR. 1993 Mar;3(2):185-204. doi: 10.1007/BF00178261.
6
Prospects for NMR of large proteins.大型蛋白质的核磁共振前景。
J Biomol NMR. 1993 Jul;3(4):375-85. doi: 10.1007/BF00176005.
7
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