Results 271 to 280 of about 492,895 (317)

Recombinant protein secretion in Escherichia coli

Biotechnology Advances, 2005
The secretory production of recombinant proteins by the Gram-negative bacterium Escherichia coli has several advantages over intracellular production as inclusion bodies. In most cases, targeting protein to the periplasmic space or to the culture medium facilitates downstream processing, folding, and in vivo stability, enabling the production of ...
F J M, Mergulhão, D K, Summers, G A, Monteiro   +2 more
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Ribosomal protein pools in Escherichia coli

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1969
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Marchis-Mouren, G., Cozzone, A., Marvaldi, J.   +2 more
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Overproduction of Escherichia coli NusA protein

Gene, 1983
The nusA gene of Escherichia coli has been cloned into the plasmid vector pKC30 under the control of the inducible lambda pL promoter. When a strain carrying this plasmid is induced, NusA protein is overproduced more than 100-fold and constitutes 20-30% of the total cellular protein.
P O, Olins, B D, Erickson, R R, Burgess
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Incorporation of fluorotryptophans into proteins of Escherichia coli

Biochemistry, 1975
A tryptophan-requiring strain of Escherichia coli can go through two doublings of optical density after L-tryptophan is replaced in the medium by 4-fluorotryptophan, during which the fluoro analog displaces approximately 75% of the L-tryptophan in cell protein.
E A, Pratt, C, Ho
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Ribosomal protein pool of Escherichia coli

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970
Abstract Escherichia coli B cells, which were grown in a heavy medium ( 15 NH 4 Cl and 2 H 2 O) and then transferred to a light medium ( 14 NH 4 Cl and 1 H 2 O), contained an expanded pool of ribosomal proteins. The expansion was attributable to the partial breakdown of ribosomes formed in the heavy medium due to the density-transfer and the ...
R M, Young, D, Nakada
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Induction of protein X in Escherichia coli

Molecular and General Genetics MGG, 1977
Certain treatments that damage DNA and/or inhibit replication in E. coli have been reported to induce synthesis of a new protein, termed protein X, in recA+ lexA+ strains. We have examined some of the treatments that might induce protein X and we have, in particular, tested the hypothesis of Gudas and Pardee (1975) that DNA degradation products play an
J W, Little, P C, Hanawalt
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Strategies for protein coexpression in Escherichia coli

Nature Methods, 2006
E. coli is a convenient host for heterologous protein expression. Its advantages include high levels of heterologous gene expression and scalability of experiments, low cost, fast growth, a lack of posttranslational modification and an ability to express labeled (isotope or seleno-methionine) proteins.
Niraj H, Tolia, Leemor, Joshua-Tor
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Membrane Protein Production in Escherichia coli

2020
Escherichia coli is the workhorse of the structural biology lab. In addition to routine cloning and molecular biology, E. coli can be used as a factory for the production of recombinant membrane proteins. Purification of homogeneous samples of membrane protein expressed in E. coli is a significant bottleneck for researchers, and the protocol we present
Benjamin C, McIlwain, Ali A, Kermani
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Phosphorylation of an Escherichia coli protein at tyrosine

Journal of Molecular Biology, 1986
The analysis of protein phosphorylation in the bacterium Escherichia coli showed that, while most phosphoproteins are modified at serine and/or threonine residues, one of them is modified exclusively at tyrosine. This particular protein which has a molecular weight of 54,500 and a pHi value of 5.6 is found associated with the membrane/ribosome fraction
Cortay, Jc, Duclos, B., Cozzone, Aj
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PROTEIN SECRETION IN ESCHERICHIA COLI

Annual Review of Microbiology, 1985
INTRO DUCT I ON . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 615 MODELS OF PROTEIN E XPORT ..... . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. . . . . . . . . . . . . .. .... . .. . ...
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