Scaling of folding times with protein size
Scaling of folding times with protein size
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DOI：
10.1021/ja044449u
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发表时间：
2005-01-19
影响因子：
15
通讯作者：
Muñoz, V
中科院分区：
文献类型：
--
作者：
Naganathan, AN;Muñoz, V
目前的实验数据显示蛋白质折叠时间跨度达 9 个数量级。如此广泛的范围通常被认为是天然蛋白质结构和序列模式复杂性的直接结果。通过使用实验分析的 69 种蛋白质和肽的数据库，我们观察到折叠时间随蛋白质中残基的数量而变化。相关系数为 0.74 或更高，表明仅根据蛋白质的大小就可以以约 1.1 倍数十年的精度预测蛋白质的折叠时间。对这种相关性的简单热力学分析表明，最小的蛋白质预计具有非常边际的折叠自由能势垒。
Current experimental data show a 9-orders-of-magnitude span in the folding times of proteins. Such a wide range is typically considered a direct consequence of the complexity in structural and sequence patterns of natural proteins. By using a database of 69 proteins and peptides analyzed experimentally, we observe that the folding time scales with the number of residues in the protein. The correlation coefficient is 0.74 or higher, and indicates that it is possible to predict the folding time of a protein with a precision of ∼1.1 times decades from just its size. A simple thermodynamic analysis of this correlation suggests that the smallest proteins are expected to have very marginal free energy barriers to folding.