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
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
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