Protein stucture under the microscope

A collaboration between La Trobe University biochemist Dr Megan Maher and Professor So Iwata of Kyoto University is mapping the architecture of proteins that sit within cell membranes.

A collaboration between La Trobe University biochemist Dr Megan Maher and Professor So Iwata of Kyoto University is mapping the architecture of proteins that sit within cell membranes.

Dr Maher’s research uses X-ray crystallography to visualise atoms and molecules and describe the three-dimensional architectures of proteins.

“An estimated 50% of drugs interact with proteins in the cell membrane, however in most cases, their method of action is unknown,” says Maher. “My research is aimed at determining these structures so that drug design can be more targeted and therefore more effective and lessen side effects.”

Maher’s research is based on long-term projects, with the average structure of a membrane protein estimated to take five years of work and a million dollars in funding.

Dr Maher and Professor Iwata, along with her fellow project researchers received an NHMRC Project Grant as well as an ARC Discovery Project Grant to apply X-ray techniques to study protein molecules in membranes.

“Dr Maher and I have a very productive collaboration,” says Professor Iwata. “Her expertise in metalloproteins at La Trobe University and our expertise in antibody production against membrane proteins in Kyoto are complementary. I hope our collaboration will be fruitful and that we can maintain this for a long time.”

The research grants allow Dr Maher to collaborate closely with Professor Iwata’s laboratory, with part of her research being carried out in Kyoto.

“Professor Iwata is a world leader in membrane protein X-ray crystallography,” says Dr Maher. “His laboratory is state of the art and he’s made major technological contributions to every step in the process. He is a true pioneer in the field. The opportunity to visit his laboratory and view his operations first hand, afforded by the La Trobe Asia funding, was invaluable. ”

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