Molecular modeling of dynamic properties of the carrier protein from the yellow mealworm Tenebrio molitor

Steroids play an important role in the life of insects. However, transport of steroids and other hydrophobic molecules through hydrophilic media requires a specialized transport system. In the yellow mealworm Tenebrio molitor that function is implemented by the carrier protein THP12. This work focuses on study of dynamic properties of apo-state protein and its complex with an ergosterol using molecular modelling. Analyses of calculated molecular dynamics trajectories for both free and ligand-bound THP12 revealed a conformational shift arising from a ligand binding. Further free binding energy and dissociation constant of a complex were determined.