The founding principles of protein folding introduced by Christian Anfinsen, together with the numerous mechanistic investigations that followed, assume that protein folding is a thermodynamically controlled process. On the other hand, this review underscores the fact that thermodynamic control is far from being the norm in protein folding, as long as one considers an extended chemical-potential landscape encompassing aggregates, in addition to native, unfolded and intermediate states. Here, we highlight the key role of kinetic trapping of the protein native state relative to unfolded, intermediate and, most importantly, aggregated states. We propose that kinetic trapping serves an important role in biology by protecting the bioactive states of a large number of proteins from deleterious aggregation. In the event that undesired aggregates were somehow formed, specialized intracellular disaggregation machines have evolved to convert any aberrant populations back to the native state, thus restoring a fully bioactive and aggregation-protected protein cohort.

中文翻译：

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蛋白质折叠中的动力学诱捕。

克里斯蒂安·安芬森（Christian Anfinsen）提出的蛋白质折叠的基本原理，以及随后进行的大量机械研究，都假定蛋白质折叠是一个热力学控制的过程。另一方面，这项综述强调了这样一个事实，即热力学控制远不是蛋白质折叠的常态，只要人们认为除了天然，未折叠和中间状态外，还包括聚集体的扩展的化学势态势。在这里，我们强调了相对于未折叠状态，中间状态和最重要的聚集状态而言，蛋白质天然状态动力学捕获的关键作用。我们建议动力学捕获通过保护大量蛋白质免受有害聚集的生物活性状态而在生物学中发挥重要作用。