Proteins are moving machines. In order to understand how their shape influences their function, we need analytical methods to probe them. The method utilized in our laboratory is hydrogen deuterium exchange mass spectrometry. Proteins exchange hydrogens in their backbones for deuterium in solution and thereby become heavier. By following the deuterium with high resolution mass spectrometry, information about conformation in solution is gained. Several areas of interest in the lab at the moment include: analysis of the conformation of proteins related to leukemia, HIV, cancer and other viral infections. We are also trying to optimize the method by building new instruments. Most all of the proteins we study are made in our laboratory.

The summer will involve working on a projected related to hydrogen exchange mass spectrometry. This could include mastering any number of analytical methods up front of the mass spectrometry measurements, in addition to learning how to make recombinant proteins in bacterial systems. Students will learn all about proteins and how to deal with them.