Using structural analysis to investigate physicochemical properties that dictate enzyme functionality

We use structural analysis tools to evaluate enzyme properties that dictate functionality. Evaluating enzyme-substrate interactions, we investigate features that contribute to the interaction of enzymes with lignin, a plant cell wall polymer that inhibits enzymatic saccharification of polysaccharides for the production of biofuel. We investigate surface properties of eight model structures and find the adsorption of enzymes to lignin correlates with solvent-exposed hydrophobic clusters. We use similar structural analysis tools to evaluate how proteins evolve to function at high temperatures. While multiple principles important for thermostability have been identified, we lack a unified understanding of how local structural and chemical environment determines quantitative impact of evolutionary mutations. We compare thermophilic and mesophilic enzymes to identify sequence and structure adaptations, revealing adaptive mechanisms under the selective pressure of high temperature.