I was introduced to research as a child, through visits to my father's nutritional biochemistry lab at UBC. My first lab job was tending white tailed deer and caribou for a study of Vitamin A deficiency. Those skittish critters enhanced my interest in math and physics! I moved to the University of Victoria after a first undergrad year in Arts and Science at UBC. The new UVic program in Bacteriology and Biochemistry was a positive change after the big intro classes at UBC...including Intro Physics with 499 UBC Engineers! At UVic classes were small and undergrads were treated like grad students - that meant high academic expectations and good interactions with faculty. Single courses in biochemistry, microbiology and molecular biology capped a program rich in organic, physical and analytical chemistry.
Since molecular biology was new and captivating I chose chromatin structure as the topic of my PhD research at the University of Edinburgh... and met my Scottish relatives. Next I accepted a Postdoctoral Fellowship in Leon Heppel's lab at Cornell University, agreed to study membrane transport in Escherichia coli, and found myself immersed in the Great Chemiosmotic Wars! By 1980 most biochemists were convinced that the protonmotive force was a key bioenergetic intermediate. But to understand how a membrane enzyme can be fuelled by protons would require understanding the structures and dynamics of integral membrane proteins - a challenge!
At Cornell and in my lab at Guelph we found that E. coli has multiple transporters for each amino acid, suggesting that each transporter has a distinct physiological role. Students Suzanne Grothe and Tom Redelmeier joined me for my first sabbatical year, in Paul Boyer's lab at UCLA. There we learned how it feels to do sophisticated enzymology on a complex molecular machine: the F0F1-ATPase. Back in Guelph we learned that two proline transporters help E. coli to survive osmotic stress - an important skill for bacteria that survive in water and food as well as human and animal tissues.
Many people now share our interest in cellular osmoregulation because it is important to all living cells, in agriculture and in medicine. But how can a (membrane) protein sense and respond to changes in the osmotic pressure of a solution? How can proline transport be coupled to the protonmotive force and linked to the osmotic pressure? Thanks to Dr. Sandy Kirk, my UVic Phys Chem Prof, we are close to answering that question...