Evolution of the folding ability of proteins through functional selection
Evolution of the folding ability of proteins through functional selection
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DOI：
10.1073/pnas.94.21.11324
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发表时间：
1997-10-14
影响因子：
11.1
通讯作者：
Yomo, T
中科院分区：
文献类型：
--
作者：
Saito, S;Sasai, M;Yomo, T
“用一个简单的蛋白质自旋玻璃样模型模拟进化过程，以检查折叠能力的起源。在每一代中，序列被随机突变，并进行基于模型的折叠过程的模拟，根据活性位点处的局部构型的频率，选择序列并传递到下一代，经过几百代，能够全局折叠成天然构象的序列出现。此外，所选择的序列具有独特的能量最小值和能量表面上的各向异性漏斗，这是蛋白质快速折叠的必要特征。所提出的模型揭示了局部构型上的功能选择导致序列以更快的速率全局折叠成构象。
`An evolutionary process is simulated with a simple spin-glass-like model of proteins to examine the origin of folding ability. At each generation, sequences are randomly mutated and subjected to a simulation of the folding process based on the model, According to the frequency of local configurations at the active sites, sequences are selected and passed to the next generation, After a few hundred generations, a sequence capable of folding globally into a native conformation emerges. Moreover, the selected sequence has a distinct energy minimum and an anisotropic funnel on the energy surface, which are the imperative features for fast folding of proteins, The proposed model reveals that the functional selection on the local configurations leads a sequence to fold globally into a conformation at a faster rate.