By A.H. Rose, D.W. Tempest (Ed.)
From the reports of prior Volumes "This sequence has continually awarded a well-balanced account of growth in microbial physiology...Invaluable for educating purposes." -AMERICAN SCIENTIST
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Additional info for Advances in Microbial Physiology, Vol. 36
Side-chain specificity was studied using a range of homo-tripeptides as competitors. g. Lys3) showed no competition, whereas peptides composed of either polar or hydrophobic side-chain residues were good competitors. Peptide-binding to OppA was also assessed using fluorescence emission spectroscopy, involving excitation at 290 nm and tryptophan-fluorescence emission at 349 nm. This technique has been used to study ligand binding to a variety of periplasmic-binding proteins (Furlong, 1987). However, neither Ala3 nor Ala-Phe-Gly caused a change in the fluorescence emission spectrum, although both had been shown to bind well by equilibrium dialysis.
B2). In all instances, mutants can be mapped to the dpp locus and a proportion are defective in synthesis of the dipeptide-binding protein. 4. The Dipeptide Binding Protein, DppA The gene, dppA, encoding the dipeptide binding protein in E. , 1991). Olson and his coworkers noted that, quite uniquely, E. coli strain JM101, grown in minimal medium, produces a protein of about 50 kDa that represents about 90% of the total periplasmic proteins. Genetic mapping showed the locus for the gene to be at 80 min.
1983). 1% (vh) trifluoroacetic acid, the protein is recovered as a sharp, ligand-free peak eluting at 40% acetonitrile (Tyreman, 1990). Many of the binding proteins have been crystallized and their tertiary structures determined using X-ray diffraction. This work has revealed strong structural similarities within this group of proteins (Quiocho, 1990, 1992). Thus, although in general binding proteins share very little sequence similarity, they do have very similar overall conformations. 0 nm.
Advances in Microbial Physiology, Vol. 36 by A.H. Rose, D.W. Tempest (Ed.)