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[求助]
帮忙改写一下这段话,保持大意基本一致，换个说法就行，自己改写的太烂了，谢谢
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| Directed evolution is considered to be the most powerful approach for improving the thermostability of proteins. In fact, comparative studies performed with hyperthermostable enzymes and their mesophilic counterparts have shown nearly superimposable three-dimensional structures suggesting that in nature extreme thermostability seems to be achieved by distributing different types of additional intramolecular interactions throughout the protein. Moreover our understanding of these interactions is incomplete and often does not allow to reliably predicting how they combine to yield a more stable protein. Therefore, rational approaches such as sited-irected mutagenesis shows often a limited efficiency and the random introduction of a small number of amino acid changes by error-prone PCR or DNA shuffling emerges as the most appropriate methodology to improve protein stability. Directed evolution method to impart non-natural properties of enzymes have found significant success recently. These strategies are based on delinking the enzyme property from its contribution to survival. Such approaches have allowed us to sample the physicochemical space of a protein instead of only its physiological space. Several proteins with special properties have been generated and also the methods required to perform such experiments have been fine-tuned. Thermal stability is a critical property for many biotechnological applications of proteins as it implies longer life-times and frequently higher tolerance to the presence of organic co-solvents, extreme pH values and high salt concentration or pressures. |
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genhunter
至尊木虫 (著名写手)
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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
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
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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. |
3楼2015-03-20 19:23:32
genhunter
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| Directed evolution is considered to be one of the most powerful approaches to improve the thermostability of a protein. In fact, studies compare hyperthermostable enzymes with their mesophilic counterparts have shown nearly superimposable 3-D structures, suggesting that in nature extreme thermostability seems to a consequence of multiple alterations in intramolecular interactions throughout the 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 purpose, using site-directed mutagenesis. 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. Introducing non-natural properties of enzymes by directed evolution method have found significant success recently. One unique advantage of such strategies is the uncoupling a phenotype due to enzyme property from its rule to cell' or organism' 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??). 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 co-solvents, extreme pH values,m high salt concentration or high pressures. |
2楼2015-03-20 18:41:33