The conformation and post-translational modification (PTM) of a protein is critically important to its function. Mass spectrometry has been increasingly utilized to analyze both of these attributes. Acidic PTMs, like phosphorylation and sulfation however, present significant obstacles to analysis. Here, I present a series of techniques to overcome these issues and improve the annotation of these vital modifications. Lastly, I discuss the use of MS-based techniques for the analysis of therapeutic protein conformation.

Sensing of ions is an integral part in bioanalysis and in the management of healthcare, water, the environment, and a range of industrial activities (e.g., agriculture and food processing). Traditionally, ion sensing was performed by sending samples to central test laboratories. Once the analysis is performed by the technician, the results are reported back to the customer or the healthcare provider.

Plastic pollution has reached alarming levels in the environment, particularly in our oceans. From documentary programs such as Blue Planet II, through to media from around the globe, the sheer scale of the problem is now receiving the attention that it deserves. One of the most common plastics, polyethylene terephthalate, or PET, is made from simple monomer building blocks that are linked together via ester bonds, hence the name polyesters.

We have examined the rapid reaction kinetics and spectroscopic properties of the molybdenum-containing, NAD+-dependent FdsABG formate dehydrogenase from C. necator, demonstrating the direct transfer of the substrate Ca hydrogen to the molybdenum center of the enzyme in the course of the reaction.

The Department of Chemistry is excited to announce the groundbreaking for our newest building, the Science, Technology, Engineering and Math Research Building, STEM-I.  The new building will house research teams from both the Chemistry Department and the Engineering College, and is strategically designed to facilitate collaboration between students, faculty, and researchers.

Of the three most common Fe-S clusters found in nature, the [4Fe-4S] cluster is the most abundant and accounts for the most diverse functions, ranging from electron transfer to regulation of gene expression and radical generation¹. Solvent accessible [4Fe-4S] clusters are very sensitive to oxidative degradation and as such, are sometimes used as sensors of oxidative stress².

This seminar will address three topics. 1: Protein PTMs that cause or contribute to neurodegenerative disease. 2: Protein PTMs that ameliorate neurodegenerative disease. 3: Cyclic thiosulfinate cross-linkers. These highly tunable S-cross-linkers avoid the toxic dead-end modifications created by previous cross-linkers, making safe in vivo cross-linking possible.