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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >An amino acid code for protein folding
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An amino acid code for protein folding

机译：蛋白质折叠的氨基酸代码

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Direct Structural information obtained for many proteins supports the following conclusions. The amino acid sequences of proteins can stabilize not only the final native state but also a small set of discrete partially folded native-like intermediates. Intermediates are formed in steps that use as units the cooperative secondary structural elements of the native protein. Earlier intermediates guide the addition of subsequent units in a process of sequential stabilization mediated by native-like tertiary interactions. The resulting stepwise self-assembIy process automatically constructs afolding pathway. whether linear or branched. These conclusions are drawn mainly from hydrogen exchange-based methods, which can depict the structure of infinitesimally populated folding inter- mediates at equilibrium and kinetic intermediates with subsecond lifetimes. Other kinetic studies show that the polypeptide chain enters the folding pathway after an initial free-energy-uphill conformational search. The search culminates by finding a native- like topology that can support forward (native-like) folding in a free-energy-downhill manner. This condition automatically de- fines an initial transition state, the search for which sets the maximum possible (two-state) folding rate. It also extends the sequential stabilization strategy, which depends on a native-like context, to the first step in the folding process. Thus the native structure naturally generates its own folding pathway. The same amino acid code that translates into the final equilibrium native strutture--by virtue of propensities. patterning, secondary struc- tural cueing, and tertiary context-also produces its kinetic accessibility.
机译：从许多蛋白质获得的直接结构信息支持以下结论。蛋白质的氨基酸序列不仅可以稳定最终的天然状态，还可以稳定一小组离散的部分折叠的天然样中间体。以天然蛋白质的协同二级结构元件为单位的步骤中形成中间体。较早的中间体在由天然样三级相互作用介导的顺序稳定过程中指导后续单元的添加。由此产生的逐步自组装过程会自动构建折叠途径。无论是线性的还是分支的。这些结论主要来自基于氢交换的方法，该方法可以描述处于平衡状态且动力学中间体具有亚秒寿命的无限同时填充的折叠中间体的结构。其他动力学研究表明，多肽链在最初的自由能上坡构象搜索后进入折叠途径。搜索通过找到可以以自由能量下坡方式支持正向折叠（类似于自然折叠）的类似于本地的拓扑而结束。此条件会自动定义一个初始过渡状态，对其进行搜索可设置最大可能的折叠状态（两个状态）。它还将依赖于类似本机上下文的顺序稳定策略扩展到折叠过程的第一步。因此，天然结构自然产生其自身的折叠途径。借助倾向性，可以将相同的氨基酸代码转化为最终的平衡天然结构。图案化，二级结构提示和第三级背景也产生了其动力学可及性。

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