Abstract
Pore-forming toxins are a class of proteins secreted by various bacterial strains that form pores on the target cell membranes, cause leakage of cellular components, and result in cell death. Upon encounter with the lipid membrane, the water-soluble monomeric form of the toxin undergoes significant conformational changes necessary to oligomerize and form pores. This study examines the process of pore formation of the two-component α-helical bacterial pore-forming toxin, YaxAB, in molecular detail using molecular dynamics (MD) simulations.
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