Porin: Difference between revisions
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<StructureSection load='2j1n' size='450' side='right' scene='Porin/Cv/1' caption='E. coli Ompc (PDB code [[2j1n]])'> | <StructureSection load='2j1n' size='450' side='right' scene='Porin/Cv/1' caption='E. coli Ompc (PDB code [[2j1n]])'> | ||
{{Clear}} | {{Clear}} | ||
[[Porin]] or '''Outer Membrane Proteins''' '''(Omps)''' act as channels which allow passive diffusion of sugars, ions and amino acids. They are beta barrel proteins which traverse the cell membrane. In ''E. coli'' they are named according to their genes: C, F, G (OmpC, OmpF, Ompg). See more details in<br /> | [[Porin]] or '''Outer Membrane Proteins''' '''(Omps)''' act as channels which allow passive diffusion of sugars, ions and amino acids. They are beta barrel proteins which traverse the cell membrane. In ''E. coli'' they are named according to their genes: C, F, G (OmpC, OmpF, Ompg). See more details in<br /> | ||
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<scene name='1a0s/Hidrophobic/1'>seen</scene> from the hydrophobic ring around the protein, this makes it possible to submerge in the lipid bilayer (hydrophobic amino acids are sandybrown, hydrophilic ones are cyan). As you can <scene name='1a0s/Hidrophobic1/1'>see</scene> the hole in the protein is made of mainly hydrophilic chains thus making it possible for the sugar to pass through (these scenes were created by Nádori Gergely). | <scene name='1a0s/Hidrophobic/1'>seen</scene> from the hydrophobic ring around the protein, this makes it possible to submerge in the lipid bilayer (hydrophobic amino acids are sandybrown, hydrophilic ones are cyan). As you can <scene name='1a0s/Hidrophobic1/1'>see</scene> the hole in the protein is made of mainly hydrophilic chains thus making it possible for the sugar to pass through (these scenes were created by Nádori Gergely). | ||
=== Gating and conduction of <scene name='Journal:JBSD:3/Cv/7'>nano-channel forming proteins</scene>, a computational approach <ref>doi 10.1080/07391102.2012.712460</ref>=== | === Gating and conduction of <scene name='Journal:JBSD:3/Cv/7'>nano-channel forming proteins</scene>, a computational approach <ref>doi 10.1080/07391102.2012.712460</ref>=== | ||
The functional units of the living systems are cells whose internal physico-chemical conditions needed for optimum function are different from that of the external medium and are maintained by hydrophobic membrane barrier and reconstituted water filled nano-pore forming proteins. The structure of these channels dictates their function to some extent and makes them to open or close in response to various conditions in the surrounding medium including pH, temperature, ionic strength, potential difference, osmotic pressure, presence of certain ligands and so on. Due to very complex and sensitive structures of these molecules to the medium and the effect of their native location, lipid Bilayer, different from soluble proteins, the molecular structure of most of membrane proteins have not been worked out at atomic level yet. The discovery of the crystal structure of certain membrane macromolecules have paved the way to understand the mechanism(s) by which they control the traffic of certain molecules through the membrane and the way they respond to the internal and external stimulus and signal transduction. | The functional units of the living systems are cells whose internal physico-chemical conditions needed for optimum function are different from that of the external medium and are maintained by hydrophobic membrane barrier and reconstituted water filled nano-pore forming proteins. The structure of these channels dictates their function to some extent and makes them to open or close in response to various conditions in the surrounding medium including pH, temperature, ionic strength, potential difference, osmotic pressure, presence of certain ligands and so on. Due to very complex and sensitive structures of these molecules to the medium and the effect of their native location, lipid Bilayer, different from soluble proteins, the molecular structure of most of membrane proteins have not been worked out at atomic level yet. The discovery of the crystal structure of certain membrane macromolecules have paved the way to understand the mechanism(s) by which they control the traffic of certain molecules through the membrane and the way they respond to the internal and external stimulus and signal transduction. | ||