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Polymer models of protein stability, folding, and interactions.

机译：蛋白质稳定性，折叠和相互作用的聚合物模型。

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The unfolded state and flexible linkers in the folded structure play essential roles in protein stability and folding and protein-protein interactions. Intrinsic to these roles is the fact that unfolded proteins and flexible linkers sample many different conformations. Polymer models may capture this and complement experiments in elucidating the contributions of the unfolded state and flexible linkers. Here I review what can be predicted from these models and how well these predictions match experiments. For example, Gaussian chain models give quantitatively reasonable predictions of the effects of residual charge-charge interactions in the unfolded state and qualitatively reasonable results for the effects of spatial confinement and macromolecular crowding on protein stability. A wormlike chain model has met with success in quantifying the effects of flexible linkers in binding affinity enhancement and in regulatory switches. In future developments, more realistic models may emerge from molecular dynamics simulations, and these models will guide experiments to advance our understanding of the unfolded state and flexible linkers.
机译：折叠结构中的未折叠状态和柔性接头在蛋白质稳定性以及折叠和蛋白质-蛋白质相互作用中起着至关重要的作用。这些作用的内在原因是未折叠的蛋白质和柔性接头会采样许多不同的构象。聚合物模型可以抓住这一点并补充实验，以阐明未折叠状态和柔性接头的作用。在这里，我回顾了可以从这些模型中预测的内容以及这些预测与实验的匹配程度。例如，高斯链模型给出了在展开状态下残余电荷-电荷相互作用的影响的定量合理预测，以及对于空间限制和大分子拥挤对蛋白质稳定性的影响的定性合理结果。蠕虫状链模型已成功量化了柔性接头在结合亲和力增强和调控开关中的作用。在未来的发展中，分子动力学模拟可能会出现更现实的模型，这些模型将指导实验以增进我们对未折叠状态和柔性接头的理解。

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