| 查看: 449 | 回复: 2 | ||
[求助]
帮忙翻译一段话，谢谢
|
| 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. |
回复此楼» 猜你喜欢
材料调剂
已经有4人回复
-
面上模板改不了页边距吧？
已经有6人回复
-
307求调剂
已经有6人回复
-
304求调剂
已经有5人回复
-
317一志愿华南理工电气工程求调剂
已经有8人回复
-
272求调剂
已经有3人回复
-
化工专硕348，一志愿985求调剂
已经有6人回复
-
292求调剂
已经有3人回复
-
290求调剂
已经有6人回复
-
295求调剂
已经有5人回复
zhenwuhuang
至尊木虫 (文学泰斗)
- 翻译EPI: 4
- 应助: 4351 (副教授)
- 金币: 10236.3
- 散金: 1
- 红花: 137
- 帖子: 65921
- 在线: 2433.7小时
- 虫号: 2227382
- 注册: 2013-01-07
- 性别: GG
- 专业: 人类营养
2楼2015-08-23 16:36:17
3楼2015-08-23 16:49:58
