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愛如風(fēng)過3610金蟲 (正式寫手)
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[求助]
幫忙翻譯一段話，謝謝
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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
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- 專業(yè): 通信理論與系統(tǒng)
【答案】應(yīng)助回帖
| 總之，這里給出的數(shù)據(jù)表明，蛋白質(zhì)魯棒性和適應(yīng)性可以通過在其中主功能約束所述扇區(qū)的稀疏，統(tǒng)稱進(jìn)化蛋白質(zhì)的結(jié)構(gòu)內(nèi)網(wǎng)絡(luò)中加載一個模型來解釋。由飽和點(diǎn)誘變，我們發(fā)現(xiàn)，扇區(qū)位置選擇性抗蝕變化時，與野生型配體的挑戰(zhàn)，但可以翻轉(zhuǎn)時，用功能上不同的配位體的挑戰(zhàn)，以促進(jìn)變化。該配體與部門之間的上位耦合顯示出有效的適配功能，通過極少的突變允許特異性相當(dāng)大的變化。一轉(zhuǎn)身，這些數(shù)據(jù)提供的部門架構(gòu)可能是自然的解決方案進(jìn)化設(shè)計的不斷波動的環(huán)境條件下的假設(shè)的支持。這樣的環(huán)境中施加的必要保持魯棒性突變和適應(yīng)性不同的選擇壓力，并已表明理論上影響演進(jìn)系統(tǒng)的設(shè)計。這將是非常重要的，現(xiàn)在實(shí)驗(yàn)測試，在選擇的條件下的波動的統(tǒng)計歷史根本限定天然蛋白質(zhì)的物理設(shè)計的概念。 |
2樓2015-08-27 12:34:57
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