Protein surface roughness accounts for binding strength of plasmepsin II inhibitors.

What is it about?

It has been previously described that roughness of surface accounts for more contacts (especially vdW contacts) than what could have been expected from a plane surface. A change in surface roughness, therefore, could provide an indirect way to assess the extent of change in possible number of contacts (vdW and polar contacts). The present work explored the calculations of surface fractal dimension (as a measure of surface roughness) and the relationship with experimental binding free energies of Plasmepsin II complexes.

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Why is it important?

Previous results seem to abide to the idea that increased roughness is correlated with interactions (protein‐protein or protein‐ligand). Instead, in the enzyme:inhibitor interaction context, a systematic study based on molecular dynamics (MD) simulations about the relationship between experimental binding free energy and binding site roughness has not been described yet.