Lead Chief Investigator

Jill E Gready Computational Proteomics, JCSMR, Australian National University

Project Title

Simulation and Phylogenetics to decipher Rubisco structure, function and evolution

Brief Description for General Publications

Simulations of mechanisms of enzyme catalysis and ligand binding, and conformational structure and dynamics of proteins, underpin applications in biotechnology, including agbiotech, and biopharmaceuticals in drug design and protein re-engineering. The major focus of our current work is on using computational simulation to define the catalytic mechanism of the enzyme Rubisco, which fixes carbon dioxide (CO2) in photosynthesis, and to define the conformational properties that influence its catalytic performance under physiologically relevant conditions. The work is part of a larger ongoing program to use this information together with other publicly available data and in combination with experiment to re-engineer, by specific mutations, Rubiscos with improved efficiency for implementation into crops with increased productivity. We use highly developed quantum mechanical (QM) and force field [molecular mechanical/ dynamical (MM/MD)] methods and combinations of these (e.g. QM/MM and QM/QM, and QM/MM within MD) for the computational components.