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Albert Lau on the Mechanics of Biological Machines


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Albert Lau on the Mechanics of Biological Machines

Interviewed by Catherine Gara
Albert Lau on the Mechanics of Biological Machines
Albert Lau is an assistant professor of biophysics and biophysical chemistry. He studies the actions and interactions of molecules in atomic detail, focusing on signaling proteins in the brain.

When did you first become interested in science?

LAU: Well, science is really just figuring out how things work, and when I was in my early teens, my biggest passions were playing the electric guitar and tennis. I enjoyed tinkering with them both, testing different strokes and strategies in tennis, and experimenting with how guitar setup, such as the height of the strings, string thickness and the bend of the neck, affected sound and playability. I liked learning how things worked on a mechanical level, and I loved reading books about these kinds of things.

How did you get from there to biophysics?

LAU: I decided to study physics in college at the University of Michigan. I did research in two different labs: one that was part of a collaboration with the famous Fermilab near Chicago, where they have a powerful particle accelerator used to study the structure of matter, and one working on the biophysics of single molecules. My fascination with biological machines led me to pursue graduate studies in biophysics. 
I did my Ph.D. at Harvard, studying the molecular architecture of a DNA repair enzyme. It has this amazing ability to read DNA and recognize when an A or a G is altered by certain modifications, which can occur at different sites on the molecule. I wanted to understand how it does that. It’s an important enzyme to understand because once it recognizes an error, it cuts that “letter” out of the DNA strand to prevent improper pairings, which can cause mutations. Then other enzymes come through and replace the missing letter with a correct one.

Did you go on to a postdoctoral fellowship from there?

LAU: Not immediately. I spent about three years at a biotech company that a former collaborator helped start. We were developing technologies for personalized medicine, like tailoring chemotherapy treatments to individual patients. I was in a small biophysics and genetics research group. 
I enjoyed my time there. There was a lot of excitement and camaraderie since it was a small company. But when it shut down, I realized that I wanted to return to academia to pursue my own research interests. I then did postdoctoral studies at the University of Chicago, where I was interested in learning about the energetics and dynamics of “moving parts” in biological machines.

And what are your research interests?

LAU: I try to figure out the molecular workings of glutamate receptors, which are proteins on the surface of neurons that “capture” the signaling molecules glutamate and glycine. They are crucial for the ability of neurons to communicate with each other.
One of our recent studies had an evolutionary angle to it. We worked with a collaborator at the National Institutes of Health who is a pioneer in the study of glutamate receptors. He identified glutamate receptorlike proteins in the recently sequenced genomes of comb jellies, which resemble jellyfish. Comb jellies don’t have brains but have a ”nerve net,” so we wanted to know if their neurons use glutamate receptors to communicate and, if so, how the receptors compare structurally and functionally with mammalian ones.
  comb jelly's glutamate receptor
The signaling molecule glycine (not shown) binds to a comb jelly’s glutamate receptor via access tunnels (orange). Specific pieces of the protein (purple) line the access tunnels. Credit: Albert Lau, Johns Hopkins Medicine

So, do comb jellies have glutamate receptors?

LAU: Yes. And from a bird’s-eye view, so to speak, their architecture looks very similar to ours. But a closer look at the inside of them shows a key difference in the area where glycine binds to the receptor: There are two amino acids that interact to form a stiff connection between the top and bottom lobes of the protein’s glycine-binding segment. Then, we figured out how that “bridge” affects the coming and going of glycine, which will be useful information if similar bridges are found within other proteins.

What do you enjoy doing outside the lab?

LAU: My favorite pastime these days is watching my young son experiment with what’s around him as he begins to figure out the world.

Albert Lau on Shape Changes in Neural Proteins

Albert Lau talks about his work to study how shape changes in important neural receptor proteins affect their function.