ИСТИНА

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.