Proteins can collapse into compact globules or form expanded, solvent-accessible, coil-like conformations. Additionally, they can fold into well-defined three-dimensional structures or remain partially or entirely disordered. Recent discoveries have shown that the tendency for proteins to collapse or remain expanded is not intrinsically coupled to their ability to fold. These observations suggest that proteins do not have to form compact globules in aqueous solutions. They can be intrinsically disordered, collapsed, or expanded, and even form well-folded, elongated structures. This ability to decouple collapse from folding is determined by the sequence details of proteins. In this review, we highlight insights gleaned from studies over the past decade. Using a polymer physics framework, we explain how the interplay among sidechains, backbone units, and solvent determines the driving forces for collapsed versus expanded states in aqueous solvents.

中文翻译：

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蛋白质的崩溃转变以及主干，侧链和溶剂相互作用之间的相互作用。

蛋白质可以折叠成紧密的小球，或形成扩展的，易接近溶剂的，盘绕状的构象。此外，它们可以折叠成定义​​明确的三维结构，或保持部分或全部无序。最近的发现表明，蛋白质折叠或保持扩展的趋势与折叠能力没有内在联系。这些观察结果表明蛋白质不必在水溶液中形成致密的小球。它们可能本质上是无序的，塌陷的或膨胀的，甚至形成折叠良好的细长结构。这种使折叠与折叠脱钩的能力由蛋白质的序列细节决定。在这篇评论中，我们重点介绍了过去十年中从研究中获得的见解。通过高分子物理框架，我们解释了侧链，主链单元，