Conformational changes due to membrane binding and channel formation by staphylococcal alpha-toxin
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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 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 ...
Insertion of some protein toxins into membranes proceeds through an unfolding step. The unfolding trigger can be the low pH in endosomes, exposure to body temperature, reduction of disulphide bonds or proteolytic cleavage occurring at the membrane surface. ...
A Ca2+ sensor based on the admittance change of synthetic membranes supported on derivatized silicon electrodes is reported. The ion-sensitive membranes consist of mixed monolayers of phospholipid and the Ca2+-ligand ETH 1001. The electrodes are characteri ...
The binding characteristics of a monoiodinated form of vasoactive intestinal peptide (M-[125I]VIP) to the membranes of astrocytes, intraparenchymal microvessels and synaptosomes were analyzed in mouse cerebral cortex. Binding to astrocytes, studied in prim ...
Pore-forming toxins, such as colicin A, are water-soluble proteins that insert into lipid bilayers. The water-soluble structure of Colicin A is known at a high resolution and this review describes the kinetic and structural steps involved in its soluble-to ...
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 ...
Time-resolved fluorescence anisotropy (FA) measurements are reported for 5 helical bilayer-spanning henicosapeptides, each contg. 1 tryptophan at sequence position 1, 6, 11, 16, or 21. The FA decay reflects 2 mol. processes in all cases: local internal flu ...
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 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 ...