First name,Last name,Preferred title,Overview,Position,Department,Individual
David,Russell,Professor,"My research focuses on proteomics, lipidomics, biophysical chemistry and application and development of mass spectrometry, such as ""label-free"" nano-particle based biosensors and novel peptide/protein isolation and purification strategies. We are also investigating the structure(s) of model peptides in an effort to better describe folding/unfolding and structure of membrane and intrinsically disordered (IDP) proteins. Peptides take on very different 2?, 3? and 4? structure, which determine or influence bio-activity. In the presence of lipid vesicles peptides can exist as solution-phase species, ""absorbed"" on lipid bilayers or ""inserted"" (as a monomer or multimer) in lipid bilayers. By what mechanism do peptides interact with lipid membranes to affect these structural changes, how do peptide-lipid interactions promote self-assembly to form intermediates that eventually yield aggregates, i.e., amyloid fibrils, or how does metal ion coordination affect the structure of metalloproteins? Mass spectrometry-based experiments, hydrogen/deuterium (H/D) exchange, chemical 'foot-printing' and gas-phase (ion-molecule and ion-ion reaction chemistry) and solution-phase chemical modifications, have expanded our abilities to address such questions, and new instrumental approaches, esp. ion mobility spectrometry (IMS) combined with enhanced molecular dynamics simulations (MDS), have become standard tools for structural-mass spectrometry studies. Over the past several years we have either acquired or developed novel, next-generation IM-MS instruments that are redefining cutting-edge structural-mass spectrometry research as well as cutting-edge computational tools essential to carry out these studies. Our new laboratories in the Interdisciplinary Life Sciences Building (ILSB) provides exciting opportunities for collaborative, interdisciplinary research with chemical-biologists, biochemists and other chemists.",Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/n280e03e6
Michael,Rosynek,Professor and Associate Department Head,"Heterogeneous catalytic processes form the basis for much of the chemical and petroleum processing industries. Solid catalysts enable reactions to occur at sufficiently high rates to be commercially feasible. In many cases, proper selection of a suitable catalyst also permits reaction pathways and product selectivities to occur that would not be kinetically possible in the absence of the catalyst. In our laboratory, we employ kinetic measurements of selected reactions, in combination with a variety of optical and surface spectroscopic and physical characterization techniques, to investigate the surface properties and detailed modes of operation of zeolites, metal oxides and supported metal catalysts.
Among the more challenging problems in the field of heterogeneous catalysis is that of selectively oxidizing small alkanes to higher hydrocarbons and oxygenates in high yields. We are currently investigating, for example, the catalyzed oxidative coupling of methane to C2hydrocarbon products. We have established that this reaction occurs via a heterogeneous-homogeneous reaction mechanism, in which the first step is homolytic cleavage of a C-H bond in methane at an O-site on the oxide catalyst surface. The resulting methyl radicals then emanate into the gas phase where they either undergo coupling to the desired C2 products or enter into a series of chain branching homogeneous reactions that lead to the formation of undesired COx products. We are employing x-ray photoelectron, FT-IR and in situ Raman spectroscopies to characterize the nature of the active sites on the catalyst surfaces. Additional studies using isotopic labelling and laser-induced fluorescence spectroscopy are providing details about the mechanism of this complex reaction system. Other projects involve studies of the direct selective oxidation of methane to oxygenates, such as formaldehyde and methanol, and to aromatic products.",Professor and Associate Department Head,Chemistry,https://scholars.library.tamu.edu/vivo/display/n9ed54600
Frank,Raushel,Distinguished Professor,"Enzymes catalyze a remarkable variety of chemical reactions with extremely high rate enhancements and very selective substrate specificity. The research efforts in our laboratory are directed towards a more complete understanding of the fundamental principles involved in enzyme-catalyzed chemistry and the dependence on protein structure. The pursuit of this information will provide the framework for the rational and combinatorial redesign of these complex molecules in an effort to exploit and develop the properties of enzyme active sites for a variety of chemical, biological, and medicinal uses. The techniques that we are using to solve these problems include steady-state and stopped-flow kinetics, NMR and EPR spectroscopy, X-ray crystallography, and the synthesis of inhibitors and suicide substrates. We are also using recombinant DNA methods to construct new proteins with novel catalytic properties. These efforts are currently being directed to the reactions catalyzed by phosphotriesterase and enzymes involves in the degradation of lignin and the metabolism of novel carbohydrates from the human gut microbiome.
The phosphotriesterase enzyme catalyzes the hydrolysis of organophosphate insecticides and other toxic organophosphate nerve agents. We have discovered that the active site of this protein consists of a unique binuclear metal center for the activation of water. We are now investigating the structure and properties of this metal center as a model system for the evolution of enzyme structure and function. Toward this end we have mutated the active site of this enzyme in a research project to create novel enzymes with the ability to detect, destroy, and detoxify various chemical warfare agents such as sarin, soman, and VX. The Raushel laboratory is also engaged in a large scale research project that is focused on the development of novel strategies for the discovery of new enzymes.",Distinguished Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/na84f2fec