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We study how proteins function and investigate how they might be modified for new and useful purposes. Our group uses directed evolution to produce mutant proteins which are then screened for enhanced function or other interesting properties. We frequently discover proteins which may be useful in industrial and environmental applications. X-ray crystallography and a variety of other techniques are used to determine the structures of proteins and better understand the detailed mechanics of protein function.
After graduating from Sydney University Professor Ollis completed a Post-doctoral period at Yale and then held faculty position at Northwestern University.
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The enzyme dihydrofolate reductase (DHFR) is an essential component of cellular metabolism. It is the target for a number of drugs, some of which are directed towards the bacterial form of the enzyme and function as antibiotics.
More about Antibiotic Resistance at the Molecular Level: New Targets for Drug Design
Eosinophils are white blood cells that respond to parasitic infections. The growth and differentiation of eosinophils is selectively regulated by the cytokine IL-5 that exerts its influence through a receptor that is formed by two peptides, referred to as the IL-5 α and β common receptors.
OPDA is a bacterial enzyme that shows considerable utility in bioremediation. In the last few years we have obtained the structure of OPDA using directed evolution to improve its expression in E. coli.
More about Enzyme Engineering with an Organophosphate Degrading Enzyme
Industrial applications of enzymes are frequently limited by the availability of large quantities of soluble protein. We have developed a procedure for selecting soluble variants of an insoluble protein.
We are interested in improving the properties of enzyme that for the glycolytic pathway. This is a central metabolic pathway that furnished the cell with energy (in the form of ATP) and numerous useful intermediates. Yeast extends this pathway as part of the process for the production of alcohol.