中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Engineering a More Thermostable Blue Light Photo Receptor Bacillus subtilis YtvA LOV Domain by a Computer Aided Rational Design Method

文献类型:期刊论文

作者Song, Xiangfei1,2; Wang, Yefei1,2; Shu, Zhiyu1,2; Hong, Jingbo1,2; Li, Tong1,2; Yao, Lishan1,2
刊名PLOS COMPUTATIONAL BIOLOGY
出版日期2013-07-01
卷号9期号:7
中文摘要 The ability to design thermostable proteins offers enormous potential for the development of novel protein bioreagents. In this work, a combined computational and experimental method was developed to increase the Tm of the flavin mononucleotide based fluorescent protein Bacillus Subtilis YtvA LOV domain by 31 Celsius, thus extending its applicability in thermophilic systems. Briefly, the method includes five steps, the single mutant computer screening to identify thermostable mutant candidates, the experimental evaluation to confirm the positive selections, the computational redesign around the thermostable mutation regions, the experimental reevaluation and finally the multiple mutations
combination. The adopted method is simple and effective, can be applied to other important proteins where other methods have difficulties, and therefore provides a new tool to improve protein thermostability.
 
 
英文摘要The ability to design thermostable proteins offers enormous potential for the development of novel protein bioreagents. In this work, a combined computational and experimental method was developed to increase the T-m of the flavin mononucleotide based fluorescent protein Bacillus Subtilis YtvA LOV domain by 31 Celsius, thus extending its applicability in thermophilic systems. Briefly, the method includes five steps, the single mutant computer screening to identify thermostable mutant candidates, the experimental evaluation to confirm the positive selections, the computational redesign around the thermostable mutation regions, the experimental reevaluation and finally the multiple mutations combination. The adopted method is simple and effective, can be applied to other important proteins where other methods have difficulties, and therefore provides a new tool to improve protein thermostability.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
学科主题仿真与模拟
类目[WOS]Biochemical Research Methods ; Mathematical & Computational Biology
研究领域[WOS]Biochemistry & Molecular Biology ; Mathematical & Computational Biology
关键词[WOS]GREEN FLUORESCENT PROTEIN ; FREE-ENERGY CALCULATIONS ; CHARGE-CHARGE INTERACTIONS ; PARTICLE MESH EWALD ; MOLECULAR-DYNAMICS ; REPORTER PROTEINS ; T4 LYSOZYME ; STABILITY ; STABILIZATION ; SIMULATION
收录类别SCI
语种英语
WOS记录号WOS:000322320200017
公开日期2014-03-21
源URL[http://ir.qibebt.ac.cn:8080/handle/337004/1634]  
专题青岛生物能源与过程研究所_仿真模拟团队
作者单位1.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Shandong Prov Key Lab Energy Genet, Qingdao, Peoples R China
2.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Key Lab Biofuels, Qingdao, Peoples R China
推荐引用方式
GB/T 7714
Song, Xiangfei,Wang, Yefei,Shu, Zhiyu,et al. Engineering a More Thermostable Blue Light Photo Receptor Bacillus subtilis YtvA LOV Domain by a Computer Aided Rational Design Method[J]. PLOS COMPUTATIONAL BIOLOGY,2013,9(7).
APA Song, Xiangfei,Wang, Yefei,Shu, Zhiyu,Hong, Jingbo,Li, Tong,&Yao, Lishan.(2013).Engineering a More Thermostable Blue Light Photo Receptor Bacillus subtilis YtvA LOV Domain by a Computer Aided Rational Design Method.PLOS COMPUTATIONAL BIOLOGY,9(7).
MLA Song, Xiangfei,et al."Engineering a More Thermostable Blue Light Photo Receptor Bacillus subtilis YtvA LOV Domain by a Computer Aided Rational Design Method".PLOS COMPUTATIONAL BIOLOGY 9.7(2013).

入库方式: OAI收割

来源:青岛生物能源与过程研究所

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