α-突触核蛋白的构象偏向性与瞬时结的形成
Conformational Biases of α-Synuclein and Formation of Transient Knots
摘要：
本文采用全原子模拟的方法研究了α-突触核蛋白动力学中的局部构象偏差。偏置与特定接触形成的频率有关。在这两种方法中，蛋白质本质上是无序的，其最强的偏好是使局部结构弯曲和转向。显溶剂构象可以大大扩展，这允许形成短暂的三叶结，深的和浅的，可能持续长达5 μs。两链自联合事件，无论是短寿命和长寿命的，是由形成接触的中央部分的序列。这部分在与胶束结合时倾向于形成螺旋。
英文摘要：
We study local conformational biases in the dynamics of α-synuclein by using all-atom simulations with explicit and implicit solvents. The biases are related to the frequency of the specific contact formation. In both approaches, the protein is intrinsically disordered, and its strongest bias is to make bend and turn local structures. The explicit-solvent conformations can be substantially more extended which allows for formation of transient trefoil knots, both deep and shallow, that may last for up to 5 μs. The two-chain self-association events, both short- and long-lived, are dominated by formation of contacts in the central part of the sequence. This part tends to form helices when bound to a micelle.
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