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首页> 外文期刊>Nature structural biology >FUNCTIONAL RAPIDLY FOLDING PROTEINS FROM SIMPLIFIED AMINO ACID SEQUENCES
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FUNCTIONAL RAPIDLY FOLDING PROTEINS FROM SIMPLIFIED AMINO ACID SEQUENCES

机译：简化氨基酸序列的功能快速折叠蛋白

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Early protein synthesis is thought to have involved a reduced amino acid alphabet. What is the minimum number of amino acids that would have been needed to encode complex protein folds similar to those found in nature today? Here we show that a small beta-sheet protein, the SH3 domain, can be largely encoded by a five letter amino acid alphabet but not by a three letter alphabet. Furthermore, despite the dramatic changes in sequence, the folding rates of the reduced alphabet proteins are very close to that of the naturally occurring SH3 domain. This finding suggests that despite the vast size of the search space, the rapid folding of biological sequences to their native states is not the result of extensive evolutionary optimization. Instead, the results support the idea that the interactions which stabilize the native state induce a funnel shape to the free energy landscape sufficient to guide the folding polypeptide chain to the proper structure. [References: 28]
机译：认为早期蛋白质合成涉及减少的氨基酸字母。编码与当今自然界相似的复杂蛋白质折叠所需的最少氨基酸数量是多少？在这里，我们显示了一个小的β-折叠蛋白，即SH3域，可以很大程度上由一个5个字母的氨基酸字母编码，而不能由一个3个字母的字母编码。此外，尽管序列发生了戏剧性的变化，但还原的字母蛋白的折叠率非常接近天然存在的SH3结构域的折叠率。这一发现表明，尽管搜索空间很大，但生物序列向其原始状态的快速折叠并不是广泛的进化优化的结果。取而代之的是，结果支持这样的想法，即稳定天然状态的相互作用将漏斗形状诱导为自由能态，足以将折叠多肽链引导至适当的结构。 [参考：28]

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