The intrinsically disordered human protein alpha-Synuclein (αS) has a prominent role in Parkinson's disease (PD) pathology. Several familial variants of αS are correlated with inherited PD. Disease mutations have been shown to have an impact on lipid membrane binding. Here, using electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling, we show that familial PD-associated variants are structurally defective in membrane binding and alter the local binding properties of the protein.

中文翻译：

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α-突触核蛋白疾病突变是结构缺陷和局部影响膜结合

内在紊乱的人类蛋白质 α-突触核蛋白 (αS) 在帕金森病 (PD) 病理学中具有重要作用。αS 的几种家族变异与遗传性 PD 相关。疾病突变已被证明对脂质膜结合有影响。在这里，使用电子顺磁共振波谱结合定点自旋标记，我们表明家族性 PD 相关变体在膜结合方面存在结构缺陷并改变蛋白质的局部结合特性。