Download Cell-Free Protein Expression by W. Antoni Kudlicki PDF

By W. Antoni Kudlicki

The function of cell-free rabbit reticulocyte expression structures in practical proteomics / Michele Arduengo, Elaine Schenborn, and Robin Hurst -- Advances in Insect-based cell-free protein expression / Uritza von Groll ... [et al.] -- benefits and functions of the batch-formatted E. coli cell-free expression approach / Julia E. Fletcher ... [et al.] -- Energetics in Escherichia coli-based batch cell-Free structures / Kalavathy Sitaraman and Deb ok. Chatterjee -- Disulfide bond formation in bacteria-based cell-free protein expression / Aaron R. Goerke and James R. Swartz -- The natural procedure: a minimum cell-free translation procedure / Bei-Wen Ying, Yoshihiro Shimizu and Takuya Ueda -- Cell-free expression methods for the construction and characterization of membrane proteins / Daniel Schwarz ... [et al.] -- Cell-free expression for protein NMR / A.J. Shaka -- Cell-free synthesis of membrane proteins for X-ray crystallography / Julia E. Fletcher ... [et al.] --, Bacterial cell-free expression platforms for high-throughput protein creation / T.V.S. Murthy, Leonardo Brizuela, and Joshua LaBaer -- Cell-free protein synthesis for protein microarrays / Gregory A. Michaud ... [et al.] -- Cell-free protein expression screening and protein immobilization utilizing protein microarrays / Matthew A. Coleman ... [et al.] -- Cell-free protein expression labeling with fluorophores / Jerzy Olejnik -- Cell-free synthesis of outlined protein conjugates through site-directed cotranslational labeling / Michael Gerrits ... [et al.] -- C-terminal labeling of proteins utilizing fluorescently conjugated puromycin derivatives / Ichiro Tabuchi -- Translation engineering and artificial biology / David A. Roth, Liza S.Z. Larsen and G. Wesley Hatfield -- sped up protein evolution utilizing ribosome show / Julie Douthwaite, Lutz Jermutus, Ronald Jackson -- program of in vitro virus

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3A, insert). Up to 40 μg active luciferase per ml reaction volume can be expressed as determined by a microtiter-based activity assay (Fig. 3A). The ability of the system to generate proteins capable of forming a protein complex was analysed in a pull-down assay with TFIIA subunits αβ and γ. Both subunits are expressed soluble in the Insect II extract (Fig. 2). For the pull-down assay, TFIIAγ was synthesized in a double-tagged form carrying a N-terminal Strep tag II and a C-terminal 6xHis tag. TFIIAαβ was N-terminally 6xHis-tagged.

A novel protein-RNA binding assay: functional interactions of the foot-and-mouth disease virus internal ribosome entry site with cellular proteins. RNA 2001; 7:114-22. 85. Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002; 295:1852-8. The Role of Cell-Free Rabbit Reticulocyte Expression Systems in Functional Proteomics 17 86. Hanes J, Pluckthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci USA 1997; 94:4937-42.

112. Cohen HM, Tawfik DS, Griffiths AD. Altering the sequence specificity of Hae III methyltransferase by directed evolution using in vitro compartmentalization. Protein Eng Des Sel 2004; 17:3-11. 113. Doi N, Kumadaki S, Oishi Y et al. In vitro selection of restriction endonucleases by in vitro compartmentalization. Nucl Acids Res 2004; 32:e95. 114. Ghadessy FJ, Holliger P. A novel emulsion mixture for in vitro compartmentalization of transcription and translation in the rabbit reticulocyte system.

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