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An investigation of the dynamics of ribosomal protein L9 using heteronuclear NMR relaxation measurements

机译：使用异核NMR弛豫测量研究核糖体蛋白L9的动力学

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The dynamic properties of ribosomal protein L9 from Bacillus stearothermophilus were investigated In solution using an analysis of nitrogen-15 longitudinal and transverse relaxation rates and amide nitrogen-proton nuclear Overhauser effects. The relaxation rates of the amide nitrogen nuclei were found to be correlated with the angle between the amide nitrogen-proton bond vectors and the long axis of the protein. This directional dependence of the nuclear relaxation rates is consistent with the protein having a highly elongated shape in solution, consistent with that observed in previous X-ray crystallographic studies of the crystalline form. Analysis of the nuclear relaxation data shows that the solvent-exposed nine-turn alpha helix connecting the two domains has a relatively high degree of order, in contrast to the connecting helix in the similarly shaped, but functionally different, calmodulin protein. The rotational correlation times associated with the amide nitrogen atoms of the N-terminal domain are on average slightly shorter than those of the C-terminal domain and connecting helix, providing evidence that the N-terminal domain exhibits some degree of independence in tumbling, in addition to other fast internal motions. The putative RNA-binding surfaces in each of the protein domains are characterized by relatively low order parameters, indicating that these are the most flexible regions of the molecule. Overall, the picture of the internal dynamics provided by nuclear relaxation measurements is similar to that obtained from a detailed study of amide proton exchange rates, but differs markedly from the picture provided by crystallographic temperature factors. The present study describes a molecule with unusual and complex dynamic properties, and supports a model where the protein functions as a "molecular strut" within the ribosome. (C) 1998 Academic Press. [References: 35]
机译：通过分析氮15的纵向和横向弛豫率和酰胺氮质子核Overhauser效应，研究了嗜热脂肪芽孢杆菌核糖体蛋白L9在溶液中的动力学特性。发现酰胺氮核的弛豫速率与酰胺氮-质子键载体和蛋白质的长轴之间的角度相关。核弛豫速率的这种方向依赖性与蛋白质在溶液中具有高度伸长的形状相一致，这与先前的晶体形式的X射线晶体学研究所观察到的一致。核弛豫数据的分析表明，与形状相似但功能不同的钙调蛋白蛋白中的连接螺旋相比，与两个结构域连接的溶剂暴露的九匝α螺旋具有相对较高的有序度。与N末端结构域的酰胺氮原子相关的旋转相关时间平均略短于C末端结构域和连接螺旋的相关时间，这提供了N末端结构域在翻滚中表现出一定程度的独立性的证据。除了其他快速的内部动作。每个蛋白质结构域中推定的RNA结合表面都具有相对较低阶的参数，表明这些参数是分子中最灵活的区域。总体而言，核弛豫测量提供的内部动力学图像与对酰胺质子交换速率的详细研究所获得的图像相似，但与晶体温度因子提供的图像明显不同。本研究描述了具有异常和复杂动态特性的分子，并支持了一种蛋白质在核糖体中充当“分子支撑物”的模型。 （C）1998年学术出版社。 [参考：35]

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