Results 281 to 290 of about 492,895 (317)

Protein secretion pathways in Escherichia coli

Current Opinion in Biotechnology, 1994
The export of proteins to the Escherichia coli periplasm is a well established system for heterologous protein production. With a better understanding of the protein export (SecA, Y-dependent) process and a greater awareness of the conditions necessary for correct folding of proteins in the periplasm, serious efforts are now being made to manipulate ...
M A, Blight, C, Chervaux, I B, Holland
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DNA Replication Proteins of Escherichia Coli

Annual Review of Biochemistry, 1978
PERSPECTIVES AND SUMMARY ..... .. .. 1163 ESCHERICHIA COLI CHROMOSOME REPLICATION ........ .. ..... ...... .... 116S In Vivo DNA Replication 1165 In Vitro DNA Replication 1166 SINGLE-STRANDED CIRCULAR DNA-DEPENDENT DNA SYNTHESIS .... 1168 Priming of Single-Stranded DNA Synthesis ..
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The stoichiometry of the ribosomal proteins of Escherichia coli

Molecular and General Genetics MGG, 1975
A ribosome preparation from E. coli made without stringent washing procedures has been shown to contain the same relative amounts of nearly all the ribosomal proteins as ribosomes in intact cells. Stoichiometric measurements on all the proteins of this preparation except for L8, L20, L31 and L34 have been made using an isotope dilution technique.
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Recombinant protein expression in Escherichia coli

Current Opinion in Biotechnology, 1999
Escherichia coli is one of the most widely used hosts for the production of heterologous proteins and its genetics are far better characterized than those of any other microorganism. Recent progress in the fundamental understanding of transcription, translation, and protein folding in E.
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Heterogeneity of protein turnover in Escherichia coli

Biochimica et Biophysica Acta (BBA) - General Subjects, 1965
Abstract An investigation has been made to determine the extent of turnover synthesis in the subcellular components of resting cells of Escherichia coli , and the extent to which this synthesis differs from that in normal growth. Estimates of turnover vary with the strain of organism examined, the condition of starvation and the amino acid used as ...
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[Protein kinase activity in Escherichia coli].

Comptes rendus des seances de l'Academie des sciences. Serie D, Sciences naturelles, 1979
When growing E. coli in a minimal medium, at least four proteins from the soluble fraction and one ribosome-associated protein are found phosphorylated at the level of their threonine and serine residues.
Manai, M., Cozzone, A.
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In vivo incorporation of an alkyne into proteins in Escherichia coli

Bioorganic & Medicinal Chemistry Letters, 2005
Using a genetic selection we identified mutants of the M. janaschii tyrosyl-tRNA synthetase that selectively charge an amber suppressor tRNA with para-propargyloxyphenylalanine in Escherichia coli. These evolved tRNA-synthetase pairs were used to site-specifically incorporate an alkynyl group into a protein, which was subsequently conjugated with ...
Alexander, Deiters, Peter G, Schultz
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Biochemical investigation of protein export in Escherichia coli

Journal of Cell Science, 1989
ABSTRACT Export of proteins from the bacterial cytoplasm to a final destination in the periplasm and outer membrane is one example of the fundamental process occurring in all cells whereby polypeptides are transferred across biological membranes.
S J, Hardy, L L, Randall
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Protein translocation in Escherichia coli

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1994
R A, Arkowitz, M, Bassilana
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Folding of Eukaryotic Proteins Produced in Escherichia Coli

1990
Although intracellular expression in E. coli may result in accumulation of the eukaryotic protein in inclusion bodies, the protein may often be recovered by first solubilizing with denaturant followed by refolding. Some general guidelines for developing a refolding procedure are apparent but the specific protocol must be empirically determined for each
R F, Kelley, M E, Winkler
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