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Escherichia ribosomes

Figure 2-125. Different isovalue-based surfaces of phenylalanine a) isoelectronic density b) molecular orbitals (HOMO-LUMO) c) isopotential surface and d) isosurface of the electron cryo-microscopic volume of the ribosome of Escherichia coii. Figure 2-125. Different isovalue-based surfaces of phenylalanine a) isoelectronic density b) molecular orbitals (HOMO-LUMO) c) isopotential surface and d) isosurface of the electron cryo-microscopic volume of the ribosome of Escherichia coii.
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. [Pg.655]

ACTH, adrenocorticotrophic hormone Met, methionine Met(O), methionine sulfoxide DTT, dithiothreitol L7, L12, Escherichia coli ribosomal proteins Met(0)-L12, L12 containing Met(O) residues a-l-PI, a-1-proteinase inhibitor Met(0)-a-l-PI, a-l-PI... [Pg.851]

Arnold, R. J. Reilly, J. P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal. Biochem. 1999, 269,105-112. [Pg.199]

Ku, J., Mirmira, R.G., Liu, L. andSanti, D.V. (1997) Expression of a functional non-ribosomal peptide synthetase module in Escherichia coli by coexpression with a phosphopantetheinyl transferase. Chemistry Biology, 4 (3), 203-207. [Pg.315]

Kaji, A. (1968). Techniques for measuring specific sRNA binding to Escherichia coli ribosomes. Methods Enzymol. 12B, 692—699. [Pg.297]

Chang, F.N., and Flaks, J.C. (1972) Specific cross-linking of Escherichia coli 30S ribosomal subunit. J. Mol. Biol. 68, 177. [Pg.1053]

Cover, J.A., Lambert, J.M., Norman, C.M., and Traut, R.R. (1981) Identification of proteins at the subunit interface of the Escherichia coli ribosome by cross-linking with dimethyl 3,3 -dithiobis(propionimi date). Biochemistry 20, 2843-2852. [Pg.1056]

Czworkowski, J., Odom, O.W., and Hardesty, B. (1991) Study of the topology of messenger RNA bound to the 30S ribosomal subunit of Escherichia coli. Biochemistry 30, 4821. [Pg.1057]

Huang, K.-H., Fainclough, R.H., and Cantor, C.R. (1975) Singlet energy transfer studies of the arrangement of proteins in the 30S Escherichia coli ribosome./. Mol. Biol. 97, 443. [Pg.1075]

Politz, S.M., Noller, H.F., and McWhirter, P.D. (1981) Ribonucleic acid-protein cross-linking in Escherichia coli ribosomes (4-azidophenyl) glyoxal, a novel heterobifunctional reagent. Biochemistry 20, 372-378. [Pg.1104]

Skold, S.-E. (1983) Chemical crosslinking of elongation factor G to the 23S RNA in 70S ribosomes from Escherichia coli. Nucleic Acids Res. 11, 4923. [Pg.1115]

Sun, T.T., Bollen, A., Kahan, L., and Traut, R.R. (1974) Topography of ribosomal proteins of the Escherichia coli 30S subunit as studied with the reversible cross-linking reagent methyl 4-mercaptobu-tyrimidate. Biochemistry 13, 2334—2340. [Pg.1119]

Zecherle, G.N. (1990) The ribosomal location and conformation of Escherichia coli protein L7/L12 studied by cysteine site directed mutagenesis and crosslinking. Doctoral Dissertation. University of California at Davis. [Pg.1131]

Ribosome activating cytotoxic proteins that irreversibly inhibit protein synthesis in cells, causing cell death. They are obtained from bacteria (Escherichia coli serotype 0157 H7). Verotoxin 1 is almost identical to shiga toxin (C16-A032) and differs only by a single amino acid. Verotoxin 2 has significant differences. [Pg.484]

The electron microscope (EM) has been used extensively in molecular biological research (1). Among its many applications, EM has been used to visualize polyribosomal structure (2), to visualize ribosome substructure (3), and to visualize the elongation factor Tu on the Escherichia... [Pg.292]

StarkH, RodninaM, Rinke-Appel J, BrimacombeR, WintermeyerW, vanHeelM. Visualization of elongation factor Tu on the Escherichia coli ribosome. Nature 1997 389 403 105. [Pg.302]

B. Lux, D. Gerard, and G. Laustriat, Tyrosine fluorescence ofS8 and S15 Escherichia coli ribosomal proteins, FEBS Lett. 80, 66-70 (1977). [Pg.58]

Ribosomes Escherichia coli Association — — — Schulz et al. (1976a)... [Pg.156]

Ribosomes are found in all organisms and consist of two unequal subunits. Prokaryotic ribosomes (e.g., those from Escherichia coli) are the most widely studied and those with which this article will be primarily concerned. The 50 S subunit of the E. coli ribosome consists of one strand each of 5 S and 23 S rRNA, and 32 different proteins. The 30 S subunit contains 16 S rRNA and 21 different proteins. [Pg.2]

Appendix Primary Structure of Escherichia coli Ribosomal Proteins... [Pg.56]

S. C., Puglisi, J. D. Structure of the A site of Escherichia coli 16 S ribosomal RNA complexed with an aminoglycoside antibiotic. Science 1996,... [Pg.337]


See other pages where Escherichia ribosomes is mentioned: [Pg.1653]    [Pg.100]    [Pg.24]    [Pg.852]    [Pg.854]    [Pg.852]    [Pg.854]    [Pg.263]    [Pg.289]    [Pg.292]    [Pg.254]    [Pg.296]    [Pg.1072]    [Pg.1081]    [Pg.1122]    [Pg.355]    [Pg.26]    [Pg.156]    [Pg.2]    [Pg.353]    [Pg.244]   
See also in sourсe #XX -- [ Pg.54 , Pg.56 ]




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Escherichia coli ribosome

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