Institute of Physics, Polish Academy of Sciences, Warsaw, Poland.
Methods Mol Biol. 2022;2340:105-120. doi: 10.1007/978-1-0716-1546-1_6.
We review the contact-based description of aggregation of intrinsically disordered proteins in coarse-grained and all-atom models. We consider polyglutamines and polyalanines at various concentrations of the peptides. We also study associations of two chains of α-synuclein and up to 20 chains of a 12-residue-long segment of protein tau. We demonstrate that the total number of two-chain association events (in an aggregate that comprises at least two chains) provides a useful measure of the propensity to aggregate. This measure is consistent, for instance, with the previously reported mass spectroscopy data. The distribution of the number of association events is given essentially by a power law as a function of the duration of these events. The corresponding exponent depends on the protein and the temperature but not on the concentration of the proteins.
我们回顾了在粗粒化和全原子模型中基于接触的无序蛋白质聚集的描述。我们考虑了不同浓度的聚谷氨酸和聚丙氨酸肽。我们还研究了两个α-突触核蛋白链和多达 20 个 12 个残基长的蛋白 tau 片段链的缔合。我们证明，两条链缔合事件（在至少包含两条链的聚集体中）的总数提供了一个有用的聚集倾向度量。例如，该度量与先前报道的质谱数据一致。关联事件数量的分布实质上是作为这些事件持续时间的幂律给出的。相应的指数取决于蛋白质和温度，但与蛋白质的浓度无关。
