The Environmental Protective Agency (EPA) monitors and regulates harmful chemical contaminants in the environment in order to reduce the detrimental effects they have on people and the environment. In order to monitor these contaminants, specifically in water and/or soil, people are required to go to the location of interest and collect samples to bring back to a laboratory to be analyzed. This process requires samples to be stored and preserved prior to analysis.

When the steepest descent pathway following a transition state structure for a given reaction splits in two, the reaction is said to involve a post-transition state bifurcation (PTSB). The presence of a PTSB presents complications for predicting product selectivity, in that a single transition state structure allows direct access to two products without any intervening minima (intermediates).

Lactic acid, a central metabolic intermediate of many cells, occurs as L- and D-isomers that are interconverted by lactate racemase. This enzyme from Lactobacillus plantarum is encoded by LarA and harbors a tethered nickel-pincer nucleotide (NPN) coenzyme derived from niacin.

Selective reactions with proteins carrying unique chemical reporters in living cells offer a powerful tool to study protein dynamics in their native environment. In this talk, I will discuss our work on the development of tetrazole and strained alkene reagents that allow rapid and site-specific protein labeling both in vitro and in living cells.

As modern electronic devices shrink, existing silicon-based technology struggles to reliably retain charge, presenting theoretical and physical limitations for these applications. Recently, ionic/electronic hybrid three-terminal memristive devices have been engineered to emulate biological synaptic functions, allowing for the concomitant storage and processing of information.

In the "bottom-up" approach, materials and devices are constructed from molecules capable of assembling themselves by principles/methods of molecular recognition.

Advancing requirements for composites having enhanced chemical, mechanical and physical properties are being met by molecular modifications of  both  filler particles and the matrix they are placed in. The presenter has enjoyed making successful contributions to a wide variety of technical problems by employing various chemical principles for particle synthesis and surface modification.

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.