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Titlebook: E. coli Gene Expression Protocols; Peter E. Vaillancourt Book 2003 Springer Science+Business Media New York 2003 Promoter.Proteomics.biosy

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发表于 2025-3-21 19:56:37 | 显示全部楼层 |阅读模式
书目名称E. coli Gene Expression Protocols
编辑Peter E. Vaillancourt
视频video
概述Includes supplementary material:
丛书名称Methods in Molecular Biology
图书封面Titlebook: E. coli Gene Expression Protocols;  Peter E. Vaillancourt Book 2003 Springer Science+Business Media New York 2003 Promoter.Proteomics.biosy
描述Peter E. Vaillancourt presents a collection of popular and emerging methodologies that take advantage of E. coli‘s ability to quickly and inexpensively express recombinant proteins. The authors focus on two areas of interest: the use of E. coli vectors and strains for production of pure, functional protein, and the use of E. coli as host for the functional screening of large collections of proteins and peptides. Among the cutting-edge techniques demonstrated are those for rapid high-level expression and purification of soluble and functional recombinant protein and those essential to functional genomics, proteomics, and protein engineering.
出版日期Book 2003
关键词Promoter; Proteomics; biosynthesis; gene expression; genes; tRNA; transcription
版次1
doihttps://doi.org/10.1385/1592593011
isbn_softcover978-1-61737-302-2
isbn_ebook978-1-59259-301-9Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media New York 2003
The information of publication is updating

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Book 2003protein, and the use of E. coli as host for the functional screening of large collections of proteins and peptides. Among the cutting-edge techniques demonstrated are those for rapid high-level expression and purification of soluble and functional recombinant protein and those essential to functional genomics, proteomics, and protein engineering.
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Die Hierarchie der kosmischen Strukturen,tion. Calmodulin is remarkably conserved throughout evolution. Amino acid sequences in multicellular organisms are nearly identical (>90% among mammals, insects and plants). Moreover, the three existing gene copies of calmodulin in humans code for proteins of identical amino acid sequence.
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Einleitung: Expatriates im Vormarsch,nt technology (.–.). The preparation of complexes generally relies on the ability to reconstitute such protein complexes from individually prepared recombinant proteins (.–.), a process that often involves refolding (.,.). This is generally not ideal, and in cases where one protein is unstable without the other (.), impossible.
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A. E. Slinkhard,G. Bascur,G. Hernández-Bravose of more than one vector. In contrast, use of a dual-expression vector eliminates the need to subclone from one vector system to another by combining the essential features of both eukaryotic and prokaryotic vectors in a single vector.
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Results: Western Expatriate Managers,eins require the oversight of molecular chaperones that bias intermediates towards productive folding rather than off-pathway self-associations (.). Changes in this delicate balance between on- and off-pathway reactions have ramifications both for human health and the study of proteins of structural interest or of commercial utility.
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Ausgangslage und Fragestellung,affinity anchors, like Ni.-nitrilotriacetic acid (Ni.-NTA) which is a powerful chelating ligand for the purification of His.-tagged proteins under native conditions. Ni-NTA affinity matrices allow to purify the protein of interest contained in a crude protein mixture at a concentration of 1% in one step to more than 95% homogeneity (.).
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