Mathematical modeling to understand the role of bivalent thrombin-fibrin binding during polymerization
Fig 3
Time of thrombin in free and bound states within AA, AP, and wild-type junctions.
Reported means and credibility intervals for quantities of interest from the stochastic binding model for various junctions and removal rates. Free and bound states of single thrombin molecules were tracked within AA junctions (γA/γA fibrin), AP junctions (γA/γ′ fibrin). Wild type fibrin was represented as a weighted average of these two cases. Thrombin was removed from the system at removal rates, kr. A) Mean time to removal starting from bound states, to either an E-domain or bivalently, fraction of mean time to removal spent (B) susceptible to removal, (C) bound to high-affinity bivalent sites, and (D) bound to low-affinity sites.