The Banaszak group is interested in studying structure/function relationships of two
broad classes of proteins:
In order to investigate these structure/function relationships, various biochemical techniques are employed, including molecular biology, protein chemistry, and enzymology. However, the most powerful tool for examining these relationships at the atomic level is macromolecular x-ray crystallography.
The molecular basis for the binding and transport of lipids is currently under investigation in several proteins, including apolipoprotein A1 (apoA1), lipovitellin, and a family of beta-barrel proteins known as intestinal lipid binding proteins (iLBPs). ApoA1 is the major protein component of high density lipoprotein (HDL) and lipovitellin is an egg yolk protein which serves as an energy source for the developing embryo. The iLBPs are not only of interest for their lipid binding and transport capabilities, but also for their potential use as "scaffolding" for protein engineering endeavors.
Among the metabolic enzymes currently being studied are fumarase, malate dehydrogenase (MDH), D-3-phosphoglycerate dehydrogenase (3-PGDH) , short chain 3-L-hydroxyacyl CoA dehydrogenase (SCHAD), and isocitrate dehydrogenase (IDH). In addition to the structural characterization of these enzymes to gain insight to their catalytic mechanisms, several other studies are being pursued in order to answer some intriguing questions. For example, protein engineering studies are now underway, which are designated to remove or modulate the regulatory domains of fumarase and 3-PGDH.