| 查看: 473 | 回复: 2 | ||
| 当前只显示满足指定条件的回帖，点击这里查看本话题的所有回帖 | ||
[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
266分，一志愿电气工程，本科材料，求材料专业调剂
已经有6人回复
-
求调剂
已经有4人回复
-
工科277分求调剂材料
已经有8人回复
-
0832食品科学与工程学硕282调剂
已经有9人回复
-
本科211，293分请求调剂
已经有8人回复
-
求调剂
已经有8人回复
-
0703化学调剂325分
已经有9人回复
-
求调剂
已经有11人回复
-
数一英一274机械调剂
已经有6人回复
-
求调剂，一志愿郑州大学材料与化工专硕，英二数二342分，求老师收留
已经有20人回复
3楼2015-08-23 16:49:58
zhenwuhuang
至尊木虫 (文学泰斗)
- 翻译EPI: 4
- 应助: 4351 (副教授)
- 金币: 10162.3
- 散金: 1
- 红花: 137
- 帖子: 65928
- 在线: 2434.8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
