Escherichia coli proteins

Hagler, Structure and energetics of ligand binding to proteins Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system, Proteins 4 31 (1988). 

LIV-protein (Escherichia coli) Outercapsid protein (Bacteriophage T4) Phosphocarrier Protein of the phosphotransferase system (Staphylococcus aureus) Plasminostreptin (Sireptomyces antifibrinolyticus)... 

Figure 7.2. Purification of an oxygen sensor protein. (A) A soiution of the protein Escherichia coli direct oxygen-sensing cyclase (Ec DosC) after it is partially purified by precipitation from a solution of salt (ammonium sulfate). (B) The same protein adsorbing onto a column packed with an anion-exchange matrix (diethylaminoethyl sepharose) at the neutral pH being used here, the matrix is retaining the protein because it carries a net negative charge.

Protein molecules extracted from Escherichia coli ribosomes were examined by viscosity, sedimentation, and diffusion experiments for characterization with respect to molecular weight, hydration, and ellipticity. These dataf are examined in this and the following problem. Use Fig. 9.4a to estimate the axial ratio of the molecules, assuming a solvation of 0.26 g water (g protein)"V At 20°C, [r ] = 27.7 cm g" and P2 = 1.36 for aqueous solutions of this polymer. 

Sulfaphenazole (684) and sulfazamet (685) are both examples of relatively short acting sulfonamides (B-80MI40406) and their antibacterial activity has been tested against Escherichia coli, the former being more effective than the latter. Sulfaphenazole also displaces sulfonyl ureas from protein binding sites on human serum albumin and consequently increases the concentration of the free (active) drug and produces a more intense reaction that may result in hypoglycemia. 

Gilliland, G.L., Quiocho, EA. Structure of the L-arabi-nose-binding protein from Escherichia coli at 2.4 A resolution. /. Mol. Biol. 146 341-362, 1981. 

Sacchettini, J.C., et al. Refined apoprotein stmcture of rat intestinal fatty acid binding protein produced in Escherichia coli. Proc. Natl. Acad. Sci. USA 86 7736-7740, 1989. 

Qnadroni, M., et al., 1996. Analy.sis of global re.spon.ses by protein and peptide fingerprinting of protein.s i.solated by two-dimensional electrophore-.sis. Application to snlfate-starvation re.sponse of Escherichia coli. European Journal of Biochemistry 239 773-781. This paper de.scribes the n.se of tandem MS in the analysis of protein.s in cell extracts. 

Garavito, R. M., et al., 1983. X-ray diffraction analysis of matrix porin, an integral membrane protein from Escherichia coli outer membrane. Journal of Nlolecular Biology 164 313—327. 

FIGURE 17. 33 A model of the flagellar motor assembly of Escherichia coli. The M ring carries an array of about 100 motB proteins at its periphery. These juxtapose with motA proteins in the protein complex that snrronnds the ring assembly. Motion of protons throngh the motA/motB complexes drives the rotation of the rings and the associated rod and helical filament. 

J. S. Pati ick and A. L. Lagu, Determination of recombinant human proinsulin fusion protein produced in Escherichia coli using oxidative sulfitolysis and two-dimensional HPLC, Chem. 64 507-511 (1992). 

Shimomura, O., and Inouye, S. (1999). The in situ regeneration and extraction of recombinant aequorin from Escherichia coli cells and the purification of extracted aequorin. Protein Expression and Purification 16 91-95. 

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