Lipid Tail Protrusion in Simulations Predicts Fusogenic Activity of Influenza Fusion Peptide Mutants and Conformational Models
Figure 2
Lipid tail protrusion is increased close to fusion-active peptides.
Protrusion probability is plotted in (a) as a function of distance from the nearest peptide for the full set of 600 trajectories, and compared with fusion kinetics (b) measured via lipid mixing for transfectants expressing each mutation replotted from Qiao et al. [2]. The protrusion probability is greatest for fusion peptides with an N-terminal glycine (X-31 wild-type). Protrusion is approximately half as likely near G1V mutant peptides (p<0.01, Kolmogorov-Smirnov test). The G1S peptide shows an intermediate behavior. Shaded areas denote 95% confidence intervals calculated using bootstrap resampling.