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本文引用的文献

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Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution.亲和钳的高度特异性的结构基础,亲和钳是通过定向结构域界面进化产生的合成结合蛋白。
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Designing switchable enzymes.设计可切换酶。
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Engineering key components in a synthetic eukaryotic signal transduction pathway.构建合成真核信号转导通路中的关键组件。
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Design and signaling mechanism of light-regulated histidine kinases.光调控组氨酸激酶的设计与信号传导机制。
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Effect of interdomain linker length on an antagonistic folding-unfolding equilibrium between two protein domains.结构域间连接子长度对两个蛋白质结构域之间拮抗折叠-去折叠平衡的影响。
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A Ca2+-sensing molecular switch based on alternate frame protein folding.一种基于交替框架蛋白质折叠的钙离子感应分子开关。
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Surface sites for engineering allosteric control in proteins.用于蛋白质变构控制工程的表面位点。
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Genetically encoded photoswitching of actin assembly through the Cdc42-WASP-Arp2/3 complex pathway.通过Cdc42-WASP-Arp2/3复合途径对肌动蛋白组装进行基因编码的光开关控制。
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Light-activated DNA binding in a designed allosteric protein.设计的变构蛋白中的光激活DNA结合
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Linking the functions of unrelated proteins using a novel directed evolution domain insertion method.使用一种新型定向进化结构域插入方法连接不相关蛋白质的功能。
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通过结构域和模块的非同源组合和重排产生新的蛋白质功能。

Generation of new protein functions by nonhomologous combinations and rearrangements of domains and modules.

机构信息

Department of Biochemistry and Molecular Biology, The University of Chicago, 929 East 57th Street, Chicago, IL 60637, United States.

出版信息

Curr Opin Biotechnol. 2009 Aug;20(4):398-404. doi: 10.1016/j.copbio.2009.07.007. Epub 2009 Aug 21.

DOI:10.1016/j.copbio.2009.07.007
PMID:19700302
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2763956/
Abstract

Generation of novel protein functions is a major goal in biotechnology and also a rigorous test for our understanding of the relationship between protein structure and function. Early examples of protein engineering focused on design and directed evolution within the constraints of the original protein architecture, exemplified by the highly successful fields of antibody and enzyme engineering. Recent studies show that protein engineering strategies which step away from these natural architectures, that is by manipulating the organization of domains and modules thus mimicking nonhomologous recombination, are highly effective in producing complex and sophisticated functions in terms of both molecular recognition and regulation.

摘要

创造新的蛋白质功能是生物技术的主要目标,也是对我们理解蛋白质结构与功能关系的严格考验。早期的蛋白质工程实例侧重于在原始蛋白质结构的限制内进行设计和定向进化,抗体工程和酶工程就是这方面非常成功的例子。最近的研究表明,通过操纵结构域和模块的组织从而模拟非同源重组,从这些自然结构中脱离出来的蛋白质工程策略在产生复杂和精细的分子识别和调控功能方面非常有效。