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The Response of Greek Key Proteins to Changes in Connectivity Depends on the Nature of Their Secondary Structure

机译:希腊关键蛋白对连接性变化的响应取决于其二级结构的性质

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What governs the balance between connectivity and topology in regulating the mechanism of protein folding? We use circular permutation to vary the order of the helices in the all-a Greek key protein FADD (Fas-associated death domain) to investigate this question. Unlike all-beta Greek key proteins, where changes in the order of secondary structure cause a shift in the folding nucleus, the position of the nucleus in FADD is unchanged, even when permutation reduces the complexity significantly. We suggest that this is because local helical contacts are so dominant that permutation has little effect on the entropic cost of forming the folding nucleus whereas, in all-beta Greek key proteins, all interactions in the nucleus are long range. Thus, the type of secondary structure modulates the sensitivity of proteins to changes in connectivity. (C) 2015 The Authors. Published by Elsevier Ltd.
机译:在调节蛋白质折叠机制中,什么决定着连接性和拓扑之间的平衡?我们使用循环置换来改变全希腊关键蛋白FADD(Fas相关死亡域)中的螺旋顺序,以研究此问题。与全β希腊语关键蛋白不同,后者的二级结构顺序改变会导致折叠核移位,即使排列显着降低了复杂性,FADD中核的位置也没有改变。我们认为这是因为局部螺旋接触占主导地位,因此排列对形成折叠核的熵成本影响很小,而在全β希腊键蛋白中,核中的所有相互作用都是长距离的。因此,二级结构的类型调节蛋白质对连通性变化的敏感性。 (C)2015作者。由Elsevier Ltd.发布

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