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首页> 外文期刊>Journal of Molecular Biology >THE ORDER OF SECONDARY STRUCTURE ELEMENTS DOES NOT DETERMINE THE STRUCTURE OF A PROTEIN BUT DOES AFFECT ITS FOLDING KINETICS
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THE ORDER OF SECONDARY STRUCTURE ELEMENTS DOES NOT DETERMINE THE STRUCTURE OF A PROTEIN BUT DOES AFFECT ITS FOLDING KINETICS

机译：二级结构元素的顺序不能确定蛋白质的结构，但会影响其折叠动力学

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We have analyzed the structure, stability and folding kinetics of circularly permuted forms of alpha-spectrin SH3 domain. All the possible permutations involving the disruption of the covalent linkage between two beta-strands forming a beta-hairpin have been done. The different proteins constructed here fold to a native conformation similar to that of wild-type protein, as demonstrated by nuclear magnetic resonance and circular dichroism. Although all the mutants have similar stabilities (they are 1 to 2 kcal mol(-1) less stable than the wild-type) their rate constants for folding and unfolding are quite different. Protein engineering, in combination with kinetics indicates that the folding pathway has been changed in the circularly permuted proteins. We conclude that neither the order of secondary structure elements, nor the preservation of any of the beta-hairpins present in this domain, is crucial for the ability of the polypeptide to fold, but they influence the folding and unfolding kinetics and could determine its folding pathway. [References: 48]
机译：我们分析了α-血影蛋白SH3域的圆形排列形式的结构，稳定性和折叠动力学。涉及破坏形成β-发夹的两个β-链之间的共价键的所有可能的排列已完成。如核磁共振和圆二色性所示，此处构建的不同蛋白质折叠成与野生型蛋白质相似的天然构象。尽管所有突变体都具有相似的稳定性（它们的稳定性比野生型低1至2 kcal mol（-1），但它们的折叠和展开速率常数却大不相同。蛋白质工程学与动力学相结合表明，环状排列的蛋白质中的折叠途径已经改变。我们得出结论，二级结构元素的顺序或该域中存在的任何β-发夹的保存对于多肽折叠的能力均至关重要，但它们会影响折叠和展开动力学，并可能决定其折叠途径。 [参考：48]

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