The staphylococcal alpha-toxin pore has a flexible conformation
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Membrane proteins fulfill many central functions in the biological membrane. The insertion process of these proteins and their structure, which are intimately linked to their function, are not yet well understood. As a model we studied three proteins recon ...
The synthesis, characterization, and membrane-transport properties of a series of benzo-15-crown-5- andp-tert-butylcalix[4]arene-substituted polysiloxanes are described. Receptor-functionalized poly(dimethylsiloxane)s, randomly substituted with up to 37 mo ...
The HIV Nef protein down-regulates the cell surface expression of CD4 and of MHC I at least in part through accelerated endocytosis. To investigate further the mechanism of this effect, we created chimeric integral membrane proteins comprising the extracel ...
For the first time, the std. free energy change, DG Deg, of a membrane-inserting protein with a leader sequence has been detd. exptl., using M13 procoat protein as an example. The partition coeff. for the distribution of the procoat protein between the aq. ...
Aerolysin is one of a large group of bacterial proteins that can kill target cells by forming discrete channels in their plasma membranes. The toxin has many properties in common with the porins of the Gram-negative bacterial outer membrane, including an e ...
A new method was presented to investigate the interactions between membrane receptors and their ligands in an artificial, reconstituted membrane system. Lipid bilayers were anchored via covalently attached thiolipids to TiO2/SiO2 waveguide surfaces to prod ...
Aerolysin, a virulence factor secreted by Aeromonas hydrophila, is representative of a group of beta-sheet toxins that must form stable homooligomers in order to be able to insert into biological membranes and generate channels. Electron microscopy and ima ...
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 ...
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. ...
Putative transmembrane helixes of membrane proteins in general and channel proteins in particular often contain proline residues which may induce a bend into an otherwise regular helical structure. Here, it is shown by fluorescence-energy-transfer measurem ...