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[求助]
帮忙翻译一段话，谢谢
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| In summary, the data presented here indicate that protein robustness and adaptability can be explained through a model in which the main functional constraints are loaded in the sector—a sparse, collectively evolving network within the protein structure. By saturation point mutagenesis, we find that sector positions selectively resist variation when challenged with wild-type ligand, but can flip to promote variation when challenged with a functionally distinct ligand. This epistatic coupling between ligand and sector underlies efficient functional adaptation, permitting considerable changes in specificity through very few mutations. Turned around, these data provide support for the hypothesis that the sector architecture might be the natural solution to design by evolution under conditions of constantly fluctuating environments. Such environments impose the need for maintaining robustness to mutation and adaptability to varying selection pressures and have been shown theoretically to influence the design of evolving systems. It will be important to now experimentally test the notion that the statistical history of fluctuations in conditions of selection fundamentally defines the physical design of natural proteins. |
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dvfire
木虫 (小有名气)
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【答案】应助回帖
| 总之，这里给出的数据表明，蛋白质鲁棒性和适应性可以通过在其中主功能约束所述扇区的稀疏，统称进化蛋白质的结构内网络中加载一个模型来解释。由饱和点诱变，我们发现，扇区位置选择性抗蚀变化时，与野生型配体的挑战，但可以翻转时，用功能上不同的配位体的挑战，以促进变化。该配体与部门之间的上位耦合显示出有效的适配功能，通过极少的突变允许特异性相当大的变化。一转身，这些数据提供的部门架构可能是自然的解决方案进化设计的不断波动的环境条件下的假设的支持。这样的环境中施加的必要保持鲁棒性突变和适应性不同的选择压力，并已表明理论上影响演进系统的设计。这将是非常重要的，现在实验测试，在选择的条件下的波动的统计历史根本限定天然蛋白质的物理设计的概念。 |
2楼2015-08-27 12:34:57
