First name,Last name,Preferred title,Overview,Position,Department,Individual
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
Abraham,Clearfield,Distinguished Professor,"Our research interests are focused in solid state and materials chemistry and encompass a wide variety of projects. An important goal is the ability to design and synthesize new materials whose structure and properties can be predicted and controlled. Layered compounds are amenable to manipulation to produce new structures because of the weak forces between layers. We have learned how to separate the layers of several classes of compounds and are reconstituting them into novel materials. For example, we have prepared staged materials in which alternating layers are hydrophobic and hydrophilic.
The surfaces of our layered materials react with a variety of molecules to bond them to the surface. We are developing such materials for drug delivery, heterogeneous catalysis, and polymer-nanoparticle composites.
Single crystal X-ray diffraction has been the key tool in elucidating the structure of solids. For many compounds, single crystals are unavailable so that indirect methods need to be used. We pioneered the solution of crystal structures from X-ray powder data and have had considerable success. The methods need to be improved and extended to more complex systems such as poorly crystallized materials. Combined use of X-ray, neutron and synchrotron methods are in progress and extension to EXAFS and amorphous scattering techniques is contemplated.",Distinguished Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/n6dc4bd81
Karen,Wooley,Distinguished Professor,"Our research activities combine organic syntheses, polymerization strategies and polymer modification reactions in creative ways to afford unique macromolecular structures, which have been designed as functional nanostructures, polymer systems having unique macromolecular architectures, and/or degradable polymers. The emphasis is upon the incorporation of functions and functionalities into selective regions of polymer frameworks. In some cases, the function is added at the small molecule, monomer, stage, prior to polymerization, whereas, in other cases, chemical modifications are performed upon polymers or at the nanostructure level; each requires a strategic balance of chemical reactivity and the ultimate composition and structure.",Distinguished Professor,Chemistry,https://scholars.library.tamu.edu/vivo/display/n7d5d2fbd
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