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Dynamic 15N{1H} NOE measurements: a tool for studying protein dynamics.
Journal of Biomolecular NMR ( IF 2.7 ) Pub Date : 2020-09-12 , DOI: 10.1007/s10858-020-00346-6
Vladlena Kharchenko 1 , Michal Nowakowski 1, 2 , Mariusz Jaremko 1 , Andrzej Ejchart 3 , Łukasz Jaremko 1
Affiliation  

Intramolecular motions in proteins are one of the important factors that determine their biological activity and interactions with molecules of biological importance. Magnetic relaxation of 15N amide nuclei allows one to monitor motions of protein backbone over a wide range of time scales. 15N{1H} nuclear Overhauser effect is essential for the identification of fast backbone motions in proteins. Therefore, exact measurements of NOE values and their accuracies are critical for determining the picosecond time scale of protein backbone. Measurement of dynamic NOE allows for the determination of NOE values and their probable errors defined by any sound criterion of nonlinear regression methods. The dynamic NOE measurements can be readily applied for non-deuterated or deuterated proteins in both HSQC and TROSY-type experiments. Comparison of the dynamic NOE method with commonly implied steady-state NOE is presented in measurements performed at three magnetic field strengths. It is also shown that improperly set NOE measurement cannot be restored with correction factors reported in the literature.



中文翻译:

动态 15N{1H} NOE 测量:研究蛋白质动力学的工具。

蛋白质中的分子内运动是决定其生物活性和与具有生物学重要性的分子相互作用的重要因素之一。15 N 酰胺核的磁弛豫允许人们在很宽的时间范围内监测蛋白质骨架的运动。15 N{ 1H} 核 Overhauser 效应对于鉴定蛋白质中的快速骨架运动至关重要。因此,精确测量 NOE 值及其准确性对于确定蛋白质骨架的皮秒时间尺度至关重要。动态 NOE 的测量允许确定 NOE 值及其由非线性回归方法的任何合理标准定义的可能误差。动态 NOE 测量可以很容易地应用于 HSQC 和 TROSY 型实验中的非氘化或氘化蛋白质。动态 NOE 方法与通常隐含的稳态 NOE 的比较在三个磁场强度下进行的测量中给出。还表明,使用文献中报告的校正因子无法恢复设置不当的 NOE 测量值。

更新日期:2020-09-12
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