Add to ORKGThe regularly arrayed outer membrane protein, Ompɿ, of Thermotoga maritima was purified to homogeneity and was characterized functionally by incorporation into artificial lipid bilayers. The polypeptide has an apparent molecular mass (Mr) of approx. 40 000 and forms stable trimers in the presence of 1% octyl-polyoxyethylene or 2% SDS which dissociate when boiling the sample. The protein has a secondary structure (predominantly ɿ-sheet) and an amino acid composition characteristic for porins. Pore-forming activity was demonstrated by porin incorporation into artificial bilayers proving that Ompɿ is a true porin: selectivity measurements showed a 4.4-fold selectivity for cations over anions. Conductivity of the porin is influenced by surfa...
Background: Porins provide diffusion channels for salts and small organic molecules in the outer mem...
AbstractThe great majority of trimeric porins of Gram-negative bacteria cannot be dissociated into m...
In Gram-negative bacteria, the Outer membrane (OM) acts as a first barrier to screen unwanted compou...
The regularly arrayed outer membrane protein, Ompɿ, of Thermotoga maritima was purified to homogene...
The regularly arrayed outer membrane protein, Ompɿ, of Thermotoga maritima was purified to homogene...
Porins, the major proteins found in the bacterial outer membrane, exhibit an unusual hollow β-barrel...
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a si...
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a si...
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a si...
Background: Porins provide diffusion channels for salts and small organic molecules in the outer mem...
Three major outer membrane proteins with apparent molecular masses of 43, 45, and 51 kDa were purifi...
OmpG, a monomeric pore-forming protein from Escherichia coli outer membranes, was refolded from incl...
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a si...
OmpG is a pore-forming protein from E. coli outer membranes. Unlike the classical outer membrane por...
Due in large part to their ability to facilitate the diffusion of a diverse range of solutes across ...
Background: Porins provide diffusion channels for salts and small organic molecules in the outer mem...
AbstractThe great majority of trimeric porins of Gram-negative bacteria cannot be dissociated into m...
In Gram-negative bacteria, the Outer membrane (OM) acts as a first barrier to screen unwanted compou...
The regularly arrayed outer membrane protein, Ompɿ, of Thermotoga maritima was purified to homogene...
The regularly arrayed outer membrane protein, Ompɿ, of Thermotoga maritima was purified to homogene...
Porins, the major proteins found in the bacterial outer membrane, exhibit an unusual hollow β-barrel...
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a si...
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a si...
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a si...
Background: Porins provide diffusion channels for salts and small organic molecules in the outer mem...
Three major outer membrane proteins with apparent molecular masses of 43, 45, and 51 kDa were purifi...
OmpG, a monomeric pore-forming protein from Escherichia coli outer membranes, was refolded from incl...
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a si...
OmpG is a pore-forming protein from E. coli outer membranes. Unlike the classical outer membrane por...
Due in large part to their ability to facilitate the diffusion of a diverse range of solutes across ...
Background: Porins provide diffusion channels for salts and small organic molecules in the outer mem...
AbstractThe great majority of trimeric porins of Gram-negative bacteria cannot be dissociated into m...
In Gram-negative bacteria, the Outer membrane (OM) acts as a first barrier to screen unwanted compou...