Copper Binding in E. Coli

Aaron Petty next to the machine in the lab

This summer, I worked independently on a copper binding study. The purpose of the study is to better understand the sites of copper-protein binding in the E. Coli proteome. This project is part of a larger collaborative effort of the Fitzgerald and Franz Research Groups to understand the molecular dynamics of copper in biological systems.

To address this question, I used Histidine H/D Exchange-Mass Spectrometry. This is an analytical chemistry method which adds a mass label to exposed histidine residues. The rate of this reaction is perturbed in the presence of ligand, which makes it applicable to this question. Histidine is of particular interest since previous work has shown that histidine is enriched in proteins which are susceptible to copper-induced protein precipitation.

This summer, I worked on the development of the method for this study, as well as peptide analysis and data processing. This means an equal distribution of work in the lab, with our advanced mass spectrometer, and working to implement a new software to analyze the mass spectrometric data.

I was also able to present my research as part of my work this summer. Early in June, I traveled to Minneapolis, where I presented at the American Society for Mass Spectrometry Annual Meeting. This was an excellent experience, both as an exercise in scientific communication and in getting to interact with many accomplished chemists.

I was also selected as the Alvin R. Crumbliss Summer Research Fellow by the Chemistry Department. This meant that I gave an oral presentation of my summer research to the department as the introduction to a poster session for all summer undergraduates doing research in the department.