First name,Last name,Preferred title,Overview,Position,Department,Individual
Francois,Gabbai,Professor,"Our research is concerned with the chemistry of both organic and organometallic polyfunctional Lewis acids. While an important component of our work deals with the synthesis of new examples of such polyfunctional Lewis acids, it is our ultimate intent to harness and utilize the cooperative effects occurring in such systems for the discovery of unusual structures, bonding modes, supramolecules and reactivities. Our research efforts present important ramifications in the domain of molecular recognition, supramolecular materials and catalysis.",Faculty Affiliate||Professor,Energy Institute||Chemistry,https://scholars.library.tamu.edu/vivo/display/n0d5d68bb
Sarbajit,Banerjee,Professor,"Much of our research program is directed at understanding the interplay between geometric and electronic structure at interfaces as well as in solid-state materials and to examine how this translates to functional properties. Our research thus spans the range from materials synthesis, mechanistic understanding of crystal growth processes, and structural characterization to device integration and mechanistic studies of catalysis and intercalation phenomena. We further seek to translate fundamental understanding of interfaces and materials to develop functional thin films and devices for a wide range of applications ranging from Mott memory to thermochromic window coatings and thin films for the corrosion protection of steel.",Professor||Faculty Fellow||Faculty Affiliate,Center for Health Systems and Design||Energy Institute||Chemistry,https://scholars.library.tamu.edu/vivo/display/n1fff3688
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
James,Batteas,Professor,"The research in our group is organized around three main projects: nanoscale materials and devices, biological surfaces and interfaces and nanotribology,
with the overarching goal of developing custom engineered surfaces and interfaces. This requires obtaining a fundamental (molecular level) understanding of the underlying chemistry and physics of the systems in question to afford rational approaches to test and develop new technologies. In much of our research we employ a range of scanned probe microscopies such as scanning tunneling microscopy (STM) and atomic force microscopy (AFM) to probe structure and to manipulate materials at the nanoscale.",Faculty Affiliate||Professor||Faculty Fellow||D. Wayne Goodman Professor of Chemistry,Center for Health Systems and Design||Energy Institute||Chemistry||Chemistry,https://scholars.library.tamu.edu/vivo/display/n413d1dff
Wenshe,Liu,Bovay Chair and Professor in Chemistry,"Our research interest is to design methods for the genetic incorporation of noncanonical amino acids into proteins in living cells and apply these methods in three major directions: deciphering functions of protein posttranslational modifications, small molecule sensing, and expanding chemical diversities of phage display libraries. To study protein posttranslational modifications, we have constructed methods for the site-specific installation of lysine acetylation and methylation in proteins and will apply them to study functional roles of these two modifications on p53, a tumor suppressor protein. We have also developed a strategy to site-specifically install two noncanonical amino acids into one protein in E. coli and are applying this approach to construct biosensors for small organic molecules and metal ions. Phage display is an efficient method to identify peptides for therapeutic interventions. However, a phage display peptide library has limited structure motifs and functional groups because only 20 natural amino acids can be used to generate a library. We plan to expand the chemical diversity of a phage display library by incorporating multiple noncanonical amino acids and chemically modifying them to extend functional diversities. Screening this unnatural phage display library against therapeutic targets such as c-Abl tyrosine kinase is expected to identify highly potent inhibitors.",Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/n5d9506ea
Christian,Hilty,Professor,"We are developing and applying Magnetic resonance techniques for the investigation of rapid processes and molecular dynamics. Hyperpolarization of nuclear spins yields unprecedented levels of signal, which enables us to acquire NMR spectra of reactions as they occur, in real time. Applications of these techniques include the fields of enzyme catalysis, reactions in organic chemistry, polymers, and more.
To enable the use of hyperpolarization in NMR, we develop new hardware and specially adapted NMR experiments, and investigate the dynamics of hyperpolarized spin systems.
Hand-in-hand with hyperpolarization, we use modern multi-dimensional NMR for the investigation of basic determinants of protein structure and function, including of membrane proteins.",Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/n83f91df7
Oleg,Ozerov,Professor,"The projects in our group typically involve transition metal or main group organometallic chemistry but are diverse and cover a wide variety of synthetic and mechanistic work. The ideal-case research scheme consists of: 1) discovery of a new reaction or a structural environment; 2) demonstration of unusual reactivity, structural, or electronic novelty; 3) application of these findings to develop a new catalytic process. The training of students in our group is not built around a narrow research theme but instead aims to help students mature into problem-solving practicing synthetic chemists through exposure to diverse research experiences.",Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/n8f8f768d
Daniel,Singleton,Professor,"The central focus of the Singleton research group is the study of organic, organometallic, and bioorganic reaction mechanisms, and the key tool that we use in these studies is the determination o kinetic isotope effects (KIEs). In the mid-1990's, we developed a method for the high precision combinatorial determination of small KIEs at natural abundance by NMR. Its direct applicability to complex unlabeled reactants makes this methodology 1-2 orders of magnitude faster than studies requiring labeling. At the same time, it is much more versatile - our technique can look at a great number of reactions that would have been impractical or impossible to study by labeling or mass spectral methods, and the choice of reactants can be readily changed in response to each new experimental result. The simultaneous determination of a complete set of 13C, 2H, and 17O isotope effects possible with our methodology provides a much greater level of information than available from conventional methods. In addition, substantial evidence has accumulated supporting the reliable accuracy of our results.",Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/na0239851
Dong,Son,Professor,"The main focus area of the research in our laboratory is (i) chemical synthesis of nanoscale hetero-structures of semiconducting and magnetic materials and (ii) real-time laser spectroscopic investigation of the dynamic electronic and magnetic properties of the nanostructures prepared from (i). Ultimately, we would like to obtain fundamental understanding of how the dynamic optical, electronic and magnetic properties in structurally complex nanoscale materials can be controlled by tuning their chemical and structural parameters. The knowledge obtained from these researches lays fundamental background essential in many practical applications, such as designing nanoscale electronic devices and light energy-harvesting materials.",Faculty Affiliate||Professor,Energy Institute||Chemistry,https://scholars.library.tamu.edu/vivo/display/nbddedc3d
Kevin,Burgess,Professor,"We use novel strategies Exploring Key Orientations (EKO) that feature datamining to compare simulated preferred conformers of chemotypes we design with key features at protein-protein interfaces. Many chemotype candidates can be screened against one PPI, or one chemotype can be screened against all the PPI interfaces in the PDB. Virtual hit chemotypes are prepared in my lab, then tested against protein-protein interactions of biomedicinal interest using an array of biophysical and cellular assays.
We also design small molecules to target cell surface receptors that are selectively overexpressed in cancer cells. Much or our work has been focused on the TrkC receptor that is particularly important to metastatic breast cancer and melanoma. Going forwards we are interested in expanding the targets to include cell surface receptors that are overexpressed when cancer cells undergo aberrant epithelial to mesenchymal transitions (EMT) to produce circulating tumor cells and cancer stem cells. Much of this work involves design and synthesis of the small molecules for this targeting.",Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/nc4a5cad4
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
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
Michael,Hall,Professor,"Our group applies ""state-of-the-art"" theoretical techniques to chemical problems of current interest to practicing inorganic, organometallic, and biological chemists. We also develop new algorithms that are especially suited to electronic structure problems in large transition metal molecules.",Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/ne91c0625
David,Bergbreiter,Professor,"Our group explores new chemistry related to catalysis and polymer functionalization using the tools and precepts of synthetic organic chemistry to prepare functional oligomers or polymers that in turn are used to either effect catalysis in a greener, more environmentally benign way or to more efficiently functionalize polymers. Often this involves creatively combining the physiochemical properties of a polymer with the reactivity of a low molecular weight compound to form new materials with new functions. These green chemistry projects involve undamental research both in synthesis and catalysis but has practical aspects because of its relevance to practical problems.
A common theme in our catalysis studies is exploring how soluble polymers can facilitate homogeneous catalysis. Homogeneous catalysts are ubiquitously used to prepare polymers, chemical intermediates, basic chemicals and pharmaceuticals. Such catalysts often use expensive or precious metals or expensive ligands or are used at relatively high catalyst loadings. The products often contain traces of these catalysts or ligands - traces that are undesirable for esthetic reasons or because of the potential toxicity of these impurities. Both the cost of these catalysts of these issues require catalyst/product separation - separations that often are inefficient and lead to chemical waste. These processes also use volatile organic solvents - solvents that have to be recovered and separated. Projects underway in our lab explore how soluble polymers can address each of these problems. Examples of past schemes that achieve this goal in a general way as highlighted in the Figure below.
We also use functional polymers to modify existing polymers. Ongoing projects involve molecular design of additives that can more efficiently modify polymers' physical properties. We also use functional polymers in covalent layer-by-layer assembly to surface polymers' surface chemistry.",Faculty Affiliate||Professor,Energy Institute||Chemistry,https://scholars.library.tamu.edu/vivo/display/nf01e95dd