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Insight into protein dynamics from nuclear magnetic relaxation studies

机译:通过核磁弛豫研究洞察蛋白质动力学

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摘要

In the review (63 references) the nuclear magnetic relaxation which is a unique experimental method giving insight into dynamic processes existing in proteins and covering a broad range of time scales was presented.This method,however,is demanding experimentally and theoretically.Exprimental methods limited to N nuclei are briefly presented and their limitations discussed.Analysis of experimental relaxation data for proteins can be done in the frame of model-free approach or applying spectral density mapping.Both those approaches are difficult for the physical interpretation of results.Besides motional parameters,some structural parameters influence relaxation rates and have to be estimated or determined.Hopefully,many problems connected with the analysis of relaxation data in proteins can be overcome with relaxation measurements at multiple magnetic fields for different isotopes like 15N,13C,and 2H.
机译:在本综述(63篇参考文献)中,提出了一种核磁共振弛豫的方法,它是一种独特的实验方法,可洞察蛋白质中存在的动态过程并涵盖广泛的时间范围。然而,该方法在实验和理论上都存在要求。简要介绍了从N核到N核的局限性,并讨论了其局限性。蛋白质的实验弛豫数据的分析可以在无模型方法的框架内进行,也可以应用光谱密度图分析法进行,这两种方法都难以对结果进行物理解释。希望,一些与蛋白质中弛豫数据分析有关的问题可以通过对15N,13C和2H等不同同位素在多个磁场中进行弛豫测量来克服。

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