Facile measurement of ¹H-¹5N residual dipolar couplings in larger perdeuterated proteins.

Facile measurement of ¹H-¹5N residual dipolar couplings in larger perdeuterated proteins.
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DOI:
10.1007/s10858-010-9441-9
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发表时间:
2010-10
影响因子:
2.7
通讯作者:
Bax A
Bax A
中科院分区:
生物学3区
文献类型:
--
作者:
Fitzkee NC;Bax A

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我们提出了一个简单的方法,ARTSY,提取1 JNH耦合和1H-15 N RDC从一组交错的二维1H-15 N TROSY-HSQC光谱,基于定量J相关的原则。与其他方法相比,ARTSY方法的主要优点是能够测量耦合而不缩放峰位置或改变TROSY光谱的窄线宽特性。该方法的准确性证明了模型系统GB 3。HIV整合酶,一个36 kDa的同源二聚体与不利的光谱特性的催化核心结构域的应用程序,证明了其实际效用。RDC测量的精度受到信噪比S/N的限制,信噪比S/N在2D TROSY-HSQC光谱中可实现,并且大约由30/(S/N)Hz给出。
We present a simple method, ARTSY, for extracting 1JNH couplings and 1H-15N RDCs from an interleaved set of two-dimensional 1H-15N TROSY-HSQC spectra, based on the principle of quantitative J correlation. The primary advantage of the ARTSY method over other methods is the ability to measure couplings without scaling peak positions or altering the narrow line widths characteristic of TROSY spectra. Accuracy of the method is demonstrated for the model system GB3. Application to the catalytic core domain of HIV integrase, a 36 kDa homodimer with unfavorable spectral characteristics, demonstrates its practical utility. Precision of the RDC measurement is limited by the signal-to-noise ratio, S/N, achievable in the 2D TROSY-HSQC spectrum, and is approximately given by 30/(S/N) Hz.
DOI: 10.1006/jmre.1998.1361
发表时间: 1998-04-01
影响因子: 2.2
作者:
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