Molecular Playground/OmpG: Difference between revisions
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OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. <scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'></scene> | OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. <scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'></scene> | ||
[[Image:OmpG Conformation.png | thumb| ]] | [[Image:OmpG Conformation.png | thumb|]] | ||
[2IWW] | [2IWW] | ||
[http://en.wikipedia.org/wiki/Outer_membrane_protein_G]. | [http://en.wikipedia.org/wiki/Outer_membrane_protein_G]. | ||
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Current applications using nanopores for protein detection [https://www.nanoporetech.com/technology/analytes-and-applications-dna-rna-proteins/protein-analysis-] | Current applications using nanopores for protein detection [https://www.nanoporetech.com/technology/analytes-and-applications-dna-rna-proteins/protein-analysis-] | ||
For additional information, see: Nanobiotechnology Review [http://www.nature.com/nnano/journal/v6/n4/full/nnano.2011.52.html] | For additional information, see: Nanobiotechnology Review [http://www.nature.com/nnano/journal/v6/n4/full/nnano.2011.52.html] | ||
<br | </br> | ||
==References== | ==References== | ||