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Team:TU Eindhoven/Background/Membrane Anchors
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<h2>Membrane Anchors: OmpX and Penn 2012 Anchor</h2> | <h2>Membrane Anchors: OmpX and Penn 2012 Anchor</h2> | ||
<p>To be able to click molecules over the entire cell surface, a protein to anchor the desired coating to the cell is needed. This protein has to be modified in such a way that it contains an azide displayed on the outside of the cell, where it can react with a DBCO-conjugate. Check also our <a href='https://2014.igem.org/Team:TU_Eindhoven/Background/SPAAC_Reaction'>SPAAC Reaction</a> Page for detailed information.</p> | <p>To be able to click molecules over the entire cell surface, a protein to anchor the desired coating to the cell is needed. This protein has to be modified in such a way that it contains an azide displayed on the outside of the cell, where it can react with a DBCO-conjugate. Check also our <a href='https://2014.igem.org/Team:TU_Eindhoven/Background/SPAAC_Reaction'>SPAAC Reaction</a> Page for detailed information.</p> | ||
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| + | <h3>Membrane Anchor Protein CPX</h3> | ||
| + | <p>OmpX (Outer Membrane Protein X) is a small, monomeric β-barrel protein that is highly expressed and very useful for protein display applications in <i>E. coli</i>. CPX (Circularly Permuted OmpX) was developed as a bacterial display methodology for N- and C-terminal display. It demonstrated to enable rapid screening of very large peptide libraries with high precision and efficiency. OmpX possesses four extracellular loops, with loops 2 and 3 forming a semi rigid β-sheets protruding from the cell surface. The native N- and C-termini were fused together by a GGSG-linker, and the newly formed N- and C-termini reside on the cell surface. This makes insertion of an unnatural amino acid fairly easy as it can be positioned before the N-terminus or after the C-terminus. By doing this, the protein itself does not have to be modified. | ||
| + | </p> | ||
</div> | </div> | ||
Revision as of 04:55, 5 October 2014
Membrane Anchors: OmpX and Penn 2012 Anchor
To be able to click molecules over the entire cell surface, a protein to anchor the desired coating to the cell is needed. This protein has to be modified in such a way that it contains an azide displayed on the outside of the cell, where it can react with a DBCO-conjugate. Check also our SPAAC Reaction Page for detailed information.
Membrane Anchor Protein CPX
OmpX (Outer Membrane Protein X) is a small, monomeric β-barrel protein that is highly expressed and very useful for protein display applications in E. coli. CPX (Circularly Permuted OmpX) was developed as a bacterial display methodology for N- and C-terminal display. It demonstrated to enable rapid screening of very large peptide libraries with high precision and efficiency. OmpX possesses four extracellular loops, with loops 2 and 3 forming a semi rigid β-sheets protruding from the cell surface. The native N- and C-termini were fused together by a GGSG-linker, and the newly formed N- and C-termini reside on the cell surface. This makes insertion of an unnatural amino acid fairly easy as it can be positioned before the N-terminus or after the C-terminus. By doing this, the protein itself does not have to be modified.
