Dataset for: Do transiently disordered and highly flexible N- and C-terminal tails accelerate the folding rates of globular proteins?

Numerous biological proteins exhibit intrinsic disorderness at their termini associated with multifarious functional roles. Here we show a surprising result that increased percent of terminal short transiently disordered regions with enhanced flexibility (TstDREF) is associated with accelerated folding rates of globular proteins. Evolutionary conservation of predicted disorderness at TstDREFs and drastic alteration of folding rates upon point-mutations suggest critical regulatory role(s) of TstDREFs in shaping the folding kinetics. TstDREFs are associated with long-range intra-molecular interactions and the percent of native secondary structural elements physically contacted by TstDREFs exhibit another surprising positive correlation with folding kinetics. These results allow us to infer probable molecular mechanisms behind TstDREF-mediated regulation of folding kinetics that challenge protein biochemists to assess by direct experimental testing.

众多生物蛋白质的末端区域存在内在无序性（intrinsic disorder），且该特性与多种功能作用密切相关。本研究揭示了一项令人意外的结论：末端短瞬时柔性无序区域（terminal short transiently disordered regions with enhanced flexibility，以下简称TstDREFs）的占比升高，与球状蛋白质的折叠速率加快呈显著正相关。TstDREFs区域预测无序性的进化保守性，以及点突变后蛋白质折叠速率的显著改变，均表明TstDREFs在调控蛋白质折叠动力学过程中发挥着关键作用。TstDREFs与长程分子内相互作用存在关联，且TstDREFs所物理接触的天然二级结构元件占比，与折叠动力学呈现出另一项令人意外的正相关关系。本研究结果可帮助我们推断TstDREF介导的折叠动力学调控背后潜在的分子机制，这一机制有待蛋白质生物化学家通过直接实验测试加以验证。