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A primary focus of Expert E. Expert's research efforts has been the determination of the mechanism of action of enzyme-catalyzed reactions. He has applied a wide range of kinetic techniques, including steady-state and pre-steady-state studies, isotope effect studies, inhibition, inactivation, pH dependent, and temperature dependent studies, to a variety of bacterial, yeast, and mammalian enzyme systems.

The study of enzyme structure and enzyme mechanisms has remained the primary objective of Expert's research efforts. A wide range of experimental approaches have been used in his enzymological studies, ranging from techniques that are quite biological in nature (such as site-directed mutagenesis), to chemical techniques (such as chemical and active-site-directed modification studies), to physical and spectroscopic techniques (such as UV/visible, fluorescence, NMR, EPR, and X-ray crystallography.

The role of metal ions in biological systems and, in particular, the function of divalent cations in enzyme-catalyzed reactions remains an important area of interest. Studies in Expert's laboratory have ranged from the structural characterization of metal-amino acid and metal-peptide complexes, to metal binding plant lectins, to metal-activated and metalloenzymes. His work in this area has also included a study of the interaction of platinum anti-cancer drugs with nucleotides, and the formation of aluminum complexes of biological ligands.

Expert's research group has developed an extensive expertise in the purification of peptides and proteins. The experimental approaches that he has used range from classical techniques (such as gel filtration and ion exchange chromatography), to affinity techniques (such as hydrophobic chromatography, dye ligand chromatography, and specific ligand immobilization), to newer HPLC purification techniques.

Expert's research group is exploring methods for the selective introduction of unnatural amino acids into enzymes with the goal of altering their substrate specificity and modifying their catalytic efficiency.

X-ray diffraction studies are a powerful tool to determine macromolecular structures at atomic resolution. The Ohio Crystallography Consortium at the Employer provides both instrumental capabilities and experimental expertise to solve protein structures. Expert's llaboratory is actively investigating the structures of a range of enzymes.