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In clinical isolates of Enterobacter cloacae, resistance to the newer beta-lactam antibiotics often results from overproduction of a cephalosporinase encoded by the beta-lactam-inducible ampC gene. Regulation of ampC is controlled by the divergently expres ...
The secondary structure of porin, maltoporin, and OmpA protein reconstituted in lipid membranes was detd. by Raman spectroscopy. The 3 proteins have similar structures consisting of 50-60% b-strand, .apprx.20% b-turn, and
The secondary structure of bacterio-opsin (BO), the retinal free protein-component of bacteriorhodopsin (BR), was detd. by Raman spectroscopy. Addnl. CD measurements revealed only negligible conformational differences between BO in apomembranes and BR in p ...
Previous models of protein p36 based on proteolytic fragments describe the tail and core as 2 noninteracting domains. However, monoclonal antibody H28 recognized a discontinuous epitope, which covers the peptide segments around serine-25 in the tail and ar ...
The secondary structure of alamethicin in lipid membranes below and above the lipid phase transition temp. Tt is detd. by Raman spectroscopy and CD measurements. In both cases structural data are obtained by fitting the exptl. spectra by a superposition of ...
The fumarate reductase of Escherichia coli is a bioenergetically important membrane-bound flavoenzyme consisting of four subunits. A and B comprise a membrane-extrinsic catalytic domain whereas C and D are hydrophobic polypeptides which link the catalytic ...
The conformation of the polypeptide melittin in lipid membranes as detd. by Raman spectroscopy is a bent a-helix formed by the mainly hydrophobic residues 1-21, and a nonhelical C-terminal segment of the hydrophilic residues 22-26. Fluorescence quenching e ...
The secondary structure of lactose permease (I) of Escherichia coli reconstituted in lipid membranes was detd. by Raman spectroscopy. The a-helix content was .apprx.70%, the b-strand content was
The outer membranes of many gram-negative bacteria contain a major heat-modifiable protein which shows serological cross-reactivity with the OmpA protein of Escherichia coli K-12. Using the cloned gene for the E. coli K12 protein as a DNA-DNA hybridization ...
