Electrostatic energies provide what is perhaps the most effective tool for structure-function correlation of biological molecules. The advances and the challenges in the field are illustrated in our many publications, considering a wide range of functional properties including pK(a)'s, redox potentials, ion and proton channels, enzyme catalysis, ligand binding and protein stability. Despite the current problems and the significant misunderstandings in the field, there is an overall progress that should lead eventually to quantitative descriptions of electrostatic effects in proteins and thus to quantitative descriptions of the function of proteins.
Professor Warshel's research has lead the field of quantitative studies of electrostatic energies in proteins. He provided the first treatments that considered the entire contributions to electrostatic free energies of proteins  and also introduced the first simplified microscopic treatment of the energy of charges in solvated proteins  and the first free energy perturbation study of a charge in a protein . His models opened the way to realistic calculations of the acid dissociation constant (pKa's), redox potentials and absolute binding energies in proteins (for reviews see  ). Warshel's concepts about the energetics of charges in protein interiors, and the meaning of dielectric constants  are now widely used. His findings and continued research have arguably provided by far the most physical connection between microscopic and macroscopic formulations through the PDLD/S-LRA formulations. Having the different levels of elctrostsic treatments in our program packages allows us to address key electrostatic proteins in an extremely powerful and reliable way, and tocontinue to push the frontiers of quantifying and understanding electrostatic energies in proteins and other biological systems.