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
Tadhg,Begley,Distinguished Professor,"The Begley Group is interested in the mechanistic chemistry and enzymology of complex organic transformations, particularly those found on the vitamin biosynthetic pathways. We are currently working on the biosynthesis of thiamin, molybdopterin, pyridoxal phosphate and menaquinone. Our research involves a combination of molecular biology, protein biochemistry, organic synthesis and structural studies and provides a strong training for students interested in understanding the organic chemistry of living systems and in pursuing careers in biotechnology, drug design or academia.
Thiamin pyrophosphate plays a key role in the stabilization of the acyl carbanion synthon in carbohydrate and amino acid metabolism. The biosyntheses of the thiamin pyrimidine and thiazole are complex and are different from any of the characterized chemical or biochemical routes to these heterocycles. We are particularly interested in cellular physiology and the mechanistic enzymology of thiamin biosynthesis. As an example of one of the complex transformations on this pathway, the figure below shows the structure of the pyrimidine synthase catalyzing the complex rearrangement of aminoimidazole ribotide (left) to the thiamin pyrimidine (right).",Distinguished Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/n498aa35b
Arthur,Laganowsky,Associate Professor,"A long-term research goal of our group is to determine the molecular basis behind protein-lipid interactions and how these interactions can modulate the structure and function of membrane proteins, including their interactions with signaling molecules. What determines the selectivity of membrane proteins towards lipids, and the coupling between lipid binding events and function remains a key knowledge gap in the field; one that if addressed will significantly advance our understanding of how lipids participate in both normal and pathophysiological processes of membrane proteins. Therefore, there is a critical need to expand our fundamental knowledge in this emerging field by applying and developing innovative approaches to elucidate how lipids modulate the structure function of membrane proteins. To this end, we are studying a number of ion channels, receptors and other types of membrane proteins.",Associate Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/n542411e4
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
Paul,Lindahl,Professor,"One of our two current research areas involves iron metabolism in mitochondria. The iron imported into these organelles is assembled into iron-sulfur clusters and heme prosthetic groups. Some of these centers are exported into the cytosol, while others are installed into mitochondrial apo-proteins. All of these processes are regulated in healthy cells, but various genetic mutations giving rise to diseases can cause iron to accumulate (e.g. Friedreich's ataxia) or become depleted (e.g. Sideroblastic anemia). We have developed a biophysical approach involving Mossbauer, electron paramagnetic resonance, and electronic absorption spectroscopy, to study the entire iron content of intact mitochondria in healthy and genetically altered cells. This Systems Biology approach allows us to characterize the ""iron-ome"" of mitochondria at an unprecedented level of detail. We are also using analytical tools (e.g. liquid chromatography) to identify complexes that are involved in ""trafficking"" iron into and out of the organelle.
Our other research area involves mathematical modeling of cellular self-replication on the mechanistic biochemical level. We collaborate on this multidisciplinary NSF-sponsored project with a mathematician at the University of Houston (Professor Jeffrey Morgan). We have developed a modeling framework that facilitates such modeling efforts, and have designed a number of very simple and symbolic in silico cells that exhibit self-replicative behavior. Our minimal in silico cell model includes just 5 components and 5 reactions. A second generation model includes a more realistic mechanism of mitotic regulation. One novel aspect of our approach is that cellular concentration dynamics impact (and are impacted by) cellular geometry. By minimizing membrane bending energies, we are now calculating cell geometry during growth and division. Our results suggest that the ""pinching"" observed in real cells is enforced by cytoskeletal structures.",Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/nc9ce621b
Jonathan,Sczepanski,Assistant Professor,"Our primary research goals are to develop and apply novel tools for studying DNA damage in the context of chromatin and to explore new avenues for RNA-based therapeutics and diagnostics. By combining expertise in chemical biology, molecular biology, and molecular evolution, our lab addresses challenges associated with studying and targeting noncoding RNAs from a unique perspective. In addition, we utilize modern chemical biology techniques to develop designer chromatin systems for studying DNA damage. We are seeking motivated individuals who wish to gain experience in chemical biology, molecular biology, and in vitro evolution techniques.",Assistant Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/ncc157d6e
Vytas,Bankaitis,Professor,"My laboratory is interested in the regulatory interfaces between novel lipid-mediated signal transduction pathways and important cellular functions. The focus of our work is the phosphatidylinositol/ phosphatidylcholine transfer proteins (PITPs), a ubiquitous but enigmatic class of proteins. Ongoing projects in the laboratory derive from a multidisciplinary approach that encompasses biochemical characterization of novel members of the metazoan PITP family, and the application of genetic, molecular and biophysical approaches to detailed structural and functional analyses of PITPs.",E.L. Wehner-Welch Foundation Chair||Professor||Professor,Cell Biology and Genetics||Biochemistry and Biophysics||Chemistry,https://scholars.library.tamu.edu/vivo/display/ncff8dc21