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【答案】应助回帖
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爱如风过3610: 金币+30, 翻译EPI+1, ★★★★★最佳答案, 谢谢，翻译的很好，膜拜中 2015-03-20 21:46:59
改了几处
Directed evolution is considered to be one of the most powerful approaches to improve the thermostability of a protein(这句话有上下连接问题). Studies comparing hyperthermostable enzymes with their mesophilic counterparts have shown nearly superimposable 3-D structures, suggesting that in nature extreme thermostability seems to be a consequence of multiple alterations in intramolecular interactions throughout protein molecules without drastic changes in global 3-D structures. Up to this point, our understanding of the interactions that lead to improved thermostability is incomplete, and there is no reliable way to predict how to make a more (thermo)stable protein through a collective of mutations by design using site-directed mutagenesis.(我试着分开讲，也许没吃透原意) Empirical approaches by introducing a small number of amino acids randomly by error-prone PCR or DNA shuffling followed by screening mutant proteins for desired properties have been the practical methodology to improve protein stability despite of the poor efficiency. On the other hand, introducing non-natural properties of enzymes by directed evolution method have found significant success recently. One unique advantage of such strategies is the uncoupling of an enzyme-associated property from its rule to cell's or organism's survival, which allows us to explore in the physicochemical dimension of a protein instead of in the physiological dimension. Several works have been published alone this direction, in which proteins with special properties have been generated and the methodology has been fine-tuned (Maybe??我试着分开讲，也许没吃透原意). Improved thermal stability is a critical property for many proteins with biotechnological applications, as it is associated with longer half-life and often higher degree of tolerance to the presence of organic solvents, extreme pH, high salt concentration or under high pressures. |
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