Many properties of intrinsically disordered proteins (IDPs), or protein regions (IDRs), are modulated by the nature of amino acid side chains as well as by local solvent exposure. We propose a set of exclusively heteronuclear NMR experiments to investigate these features in different experimental conditions that are relevant for physiological function. The proposed approach is generally applicable to many IDPs/IDRs whose assignment is available in the Biological Magnetic Resonance Bank (BMRB) to investigate how their properties are modulated by different, physiologically relevant conditions. The experiments, tested on α‐synuclein, are then used to investigate how α‐synuclein senses Ca²⁺ concentration jumps associated with the transmission of nerve signals. Novel modules in the primary sequence of α‐synuclein optimized for calcium sensing in highly flexible, disordered protein segments are identified.

中文翻译：

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通过专有的异核核磁共振实验监测α-突触核蛋白与钙离子的相互作用。

内在无序的蛋白质（IDP）或蛋白质区域（IDR）的许多特性受到氨基酸侧链的性质以及局部溶剂暴露的调节。我们提出了一组专门的异核NMR实验，以研究与生理功能相关的不同实验条件下的这些特征。提议的方法通常适用于许多IDP / IDR，其分配可在生物磁共振库（BMRB）中进行，以研究如何通过不同的生理相关条件调节其特性。然后，在α-突触核蛋白上进行了实验，然后用于研究α-突触核蛋白如何感知Ca ²⁺浓度跳跃与神经信号的传递有关。确定了针对α-突触核蛋白的一级序列进行了优化的新型模块，这些模块可用于高度灵活，无序的蛋白质片段中的钙感测。