Jonathan Yang, an undergraduate researcher in the Chowdhury Lab won 1st place in the Biochemistry and Chemistry Department Undergraduate Research Symposium. His work explores new methods for enriching the detection of protein N-terminal ends deemed highly important in the regulation of protein function. Some of the work in Mr. Yang's presentation was accomplished in the Shimadzu Center for Advanced Analytical Chemistry.
When a protein is synthesized by the ribosomes within our body, they are designed to serve a specific function within the cell. However, when an enzyme modifies the protein, it changes the functions of the protein and their interactions with other proteins. These changes in the protein-protein interactions then result in some of the diseases found in humans. A common site for modification by an enzyme is at the N-Terminus of a protein; therefore, our goal in this research is to isolate and analyze the sequence of the original N-Terminals of four proteins: RNAse S, Ubiquitin, Beta-casein and Bovine Serum Albumin. The four step reaction consists of first converting the primary amine of the lysine residues to homoarginine and then subsequent acetylation of the original N-terminus with acetic anhydride. After these two modifications, the mixture will undergo tryptic digest followed by biotin capture to separate the original N-terminals from the newly formed N-terminals.
Improving detection of Protein Modifications at the N-terminus