Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality
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Aerolysin is a cytolytic toxin which forms channels in the plasma membranes of eucaryotic cells. The protein is secreted by Aeromonas hydrophila as an inactive protoxin. Its stability and water solubility are conferred by its ability to dimerize. Maturatio ...
The conformations of melittin, porin, and lactose permease reconstituted in liposomal membranes were investigated by Raman spectroscopy, and the folding of membrane domains was predicted. These data resulted in consistent models for the insertion of the pr ...
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 ...
Oligomerization is a necessary step in channel formation by the bacterial toxin aerolysin. We have identified a region of aerolysin containing two tryptophans which influence the ability of the protein to oligomerize. Changing the tryptophan at position 37 ...
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 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 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
