Pore Formation: Difference between revisions

After binding to the membrane, the pore-forming domain unfolds and releases the hydrophobic helices to initiate insertion. This unfolding is shown to be linked to a low pH. 3 conserved aspartate residues in the domain form a hydrogen-bonding domain which is disrupted by the low pH, as is a critical salt bridge required for stability of the folded protein. This causes local unfolding of a helix. The helices then loosely associate on the surface of the membrane, as the hydrophobic hairpin inserts into the bilayer<ref> PMID: 16563740 </ref>.

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