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Voltage gating in porin channels [PDF]
FEBS Letters, 1987 Data from experiments in which porin channels are reconstituted into planar bilayer membranes are reviewed for their relevance to porin channel gating in vivo. Contradictory evidence concerning voltage gating indicates that the different results may stem from the variety of purification techniques employed.
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Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1
Microbiology, 1995The porin of Rhodospirillum rubrum FR1 was found in the outer membrane as a complex with a relatively small (32 kDa) porin-associated protein (PAP). The porin moiety of the complex consisted of a trimer which revealed a mainly β-sheet structure, while the porin-PAP complex also contained a significant α-helical portion.
U. Neumann +4 more
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A light-triggered transmembrane porin
Chemical Communications, 2018Porins are ideal model systems for channel engineering. Here, we present a photocaged diethylaminocoumarin (DEACM) hybrid of the transmembrane porin OmpG.
J. Kahlstatt +5 more
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Porins in the Cell Wall of Mycobacteria
Science, 1992The cell wall of mycobacteria is an efficient permeability barrier that makes mycobacteria naturally resistant to most antibiotics. Liposome swelling assays and planar bilayer experiments were used to investigate the diffusion process of hydrophilic molecules through the cell wall of Mycobacterium chelonae and ...
J, Trias, V, Jarlier, R, Benz
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1995
The mitochondrial outer membrane contains a permeability channel that is responsible for the passage of hydrophilic compounds across the membrane. The transmembrane protein, called mitochondrial porin is not particularly hydrophobic and its primary structure does not contain any indication for the existence of transmembrane hydrophobic α-helical ...
Roland Benz +3 more
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The mitochondrial outer membrane contains a permeability channel that is responsible for the passage of hydrophilic compounds across the membrane. The transmembrane protein, called mitochondrial porin is not particularly hydrophobic and its primary structure does not contain any indication for the existence of transmembrane hydrophobic α-helical ...
Roland Benz +3 more
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Biophysics of the structure and function of porins
Quarterly Reviews of Biophysics, 1990Gram-negative bacteria such asEscherichia coli(E. coli) andSalmonella typhimurium(S. typhimurium) have two layers of membranes in the cellular envelope – the cytoplasmic membrane and the outer membrane (Fig. I). Between these membranes is a periplasmic space in which there is a peptidoglycan layer that provides the cells with mechanical rigidity.
B K, Jap, P J, Walian
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Historiallinen Aikakauskirja, 1958
Arvosteltu teos: Porin historia 1-2 (Osa 1: Satakunnan varhaiskauppa ja Porin edeltäjät / Jalmari Jaakkola. Osa 2: 1558-1809 / J. W. Ruuth, uuden suomenkielisen laitoksen toim. Mauno Jokipii.)
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Arvosteltu teos: Porin historia 1-2 (Osa 1: Satakunnan varhaiskauppa ja Porin edeltäjät / Jalmari Jaakkola. Osa 2: 1558-1809 / J. W. Ruuth, uuden suomenkielisen laitoksen toim. Mauno Jokipii.)
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Structure and functional mechanism of porins
Physiological Reviews, 1996Cellular organisms such as gram-negative bacteria are enclosed by a dual lipid bilayer system. The outer membranes of the dual bilayer envelopes predominantly contain large numbers of water-filled transmembrane protein channels known as porins. The recent availability of the molecular structures of several bacterial porins has provided the opportunity
B K, Jap, P J, Walian
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The biogenesis and function of eukaryotic porins
Experientia, 1990Like most other mitochondrial proteins porin is synthesized in the cytosol and imported posttranslationally into the outer mitochondrial membrane. This transport follows the general rules for mitochondrial protein import with a few aberrations: a) porin contains an uncleaved NH2-terminal signal sequence, b) also its carboxyterminus might be involved in
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Bacterial porins: structure and function
Current Opinion in Cell Biology, 1993Within the class of integral membrane proteins, the bacterial porins display a remarkable resistance to denaturants and proteases. This stability is probably crucial for the formation of highly ordered, three-dimensional crystals. Structural analysis of these crystals has been possible in atomic detail.
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