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. 2011 Oct 6;7(10):e1002280. doi: 10.1371/journal.ppat.1002280

Figure 5. Identification of single substitutions within TgACTI that affect filament stability.

Figure 5

(A) Modeling of S199-D179 hydrogen bond and M269 in the hydrophobic loop of mammalian actin (B) Modeling of loss of hydrogen bond with G200 substitution and reduced hydrophobicity at position 270 in TgACTI. (C) Expression of TgACTI recombinant proteins containing mammalian-like substitutions in baculovirus, resolved using a 12% SDS-PAGE gel, and stained with SYPRO Ruby. (D) Comparison of polymerization kinetics of TgACTI substitutions. F buffer was added at time = 0 sec to induce polymerization of 5 µM actin and polymerization was monitored by light scattering.