Chemistry Professor 
Philip Johnson (right) is working on the cutting edge of genome research and hopes his work will one day lead to improved anti-viral drug therapies.
Johnson delves into the structure and biological function of protein and RNA (ribonucleic acid) molecules. He is engaged in the next stage of genome research – understanding the function of the molecules encoded by a genome, the genetic material of an organism.
Pharmaceutical companies are increasingly recognizing RNA molecules as important targets for drug development. And Johnson is collaborating with one of them, MCR Research.
The Canada Foundation for Innovation recently sent a certificate of congratulations to Johnson, one of several York faculty members who have received CFI grants during the past year. The CFI is an independent corporation set up by the federal government in 1997.
Johnson studies the structure and biological function of proteins, RNA and protein-RNA complexes, using such tools as nuclear magnetic resonance. Because the function of biomolecules is governed by their three-dimensional shape, he says knowing a molecule’s structure can lead to development of compounds that bind to them and disrupt their normal function, such as interfering with the life cycle of a virus.
More specifically, Johnson examines the complex between the SelB protein and an RNA "hairpin" that directs the entry of the rare amino acid selenocysteine into proteins. Understanding this interaction is the first step to designing a system to introduce such amino acids into proteins. He is also defining the mechanism by which an HIV protein functions during reverse transcription of the viral genome.