"Applying conventional disciplines of chemistry to current and future issues."



Biochemical & Biophysical Sciences




3D structure of protein
Roger Acey's group is interested in the biochemistry and genetics of early development. They use the brine shrimp Artemia to study the role of posttranslational modifications of nuclear proteins. In particular, they are interested in identifying glycosylation/methylation patterns of histone H1 and RNA Polymerase II and how they relate to changes in the rate of gene transcription during development. A second project using Artemia is focused on understanding how organisms control trace metal homeostasis, e.g., ensure the bioavailability of essential metals such as zinc while simultaneously preventing the buildup of metal to levels toxic to the cell. They have isolated a unique metal binding protein and its gene from Artemia. They believe the protein functions as an intracellular storage depot for trace metals. Since several nuclear proteins are zinc metalloproteins, the availability of zinc can regulate gene transcription. The group is interested in the mechanism by which metallothionein is able to donates zinc to nuclear apo zinc metalloproteins. Lastly, this group is focused on studying the role of butyrylcholinesterase in early development and cell differentiation. Using umbilical cord stem cells as a model biological system, they have shown that the enzyme is expressed during neural tissue formation. They are interested in clarifying the biochemical mechanisms responsible for expression of the butyrylcholinesterase and the function of the enzyme in neural tissue development.



a biomolecular structure




Jeff Cohlberg's past research has focused on problems related to protein assembly, including assembly of bacterial ribosomes from their component RNA and protein molecules, assembly of neurofilaments and other intermediate filaments from their protein subunits, and assembly of amyloid fibrils from natively folded proteins. These problems have been studied by the application of techniques of physical biochemistry, including analytical ultracentrifugation, fluorescence, infrared and circular dichroism spectroscopy, and electron microscopy. His most recent work has focused on the aggregation of superoxide dismutase as a result of mutations related to amyotrophic lateral sclerosis.



cartoon display of a protein



Doug McAbee's research interests focus on iron metabolism and iron-binding proteins. For many years, his group's work has been to understand the structure-function relationships of the iron-binding protein lactoferrin and the molecular basis for lactoferrin.s interaction with cells, particularly liver hepatocytes. More recently, this work has expanded to include an understanding of the proteomic changes that occur in liver cells during acute iron overload by mass spectrometry. In collaboration with Dr. Editte Gharakhanian (Department of Biological Sciences) they examine the function of a recently identified protein in yeast, env7, which when mutated disrupts protein trafficking between the post-Golgi network and the vacuole in yeast cells.



ApoE a cholesterol protein diagram

Vas Narayanaswami's group examines structure-function relationships of apoE using fluorescence spectroscopy and other biophysical approaches. ApoE is an important cholesterol transport protein in the plasma and brain. While the high-resolution structure of the N-terminal domain of apoE has been available for about two decades, we still do not have an understanding of the C-terminal domain, which is primarily responsible for cholesterol efflux from macrophages, or of the intact protein. Her group uses biophysical approaches such as fluorescence and circular dichroism spectroscopy to fill this gap in knowledge. The group also investigates the structural and functional basis of the isoform-specific role of apoE in Alzheimer.s disease and its role in amyloid pathology. Lastly, this group evaluates the effect of age- and environment-related oxidative stress on apoE structure and function, specifically the effect of second hand smoke exposure and the potential risk for predisposing exposed subjects to heart disease.



a technique for electrical detection of SNPs

Kris Slowinski's research group is interested in developing new experimental strategies for the electrical detection of single-nucleotide polymorphisms (SNPs) and sequence-specific DNA-binding proteins (e.g. TATA binding protein), both at the nanoscopic (single molecules) and mesoscopic (monolayers) level via monitoring of the electrical properties of DNA molecules modified with redox intercalators in electrochemically controlled tunnel junctions. Our key objective is to determine whether disruption of the DNA p-stack via a single-point mutation or a protein binding results in an analytically effectual decrease in electrical conductivity of the helix.



enzymology


Jason Schwans' research group is interested in understanding the energetic and structural basis of enzyme catalysis. Knowledge of how enzymes work is crucial to understanding biological function and may aid the design and application of enzymes and enzyme inhibitors that act as drugs. We are employing a battery of functional and structural approaches including atomic level mutagenesis using unnatural amino acids and nucleotides and x-ray crystallography. Specific topics being studied include: i) investigation of cholesterol oxidase to address how general acid/base catalysis contributes to enzymatic rate enhancement when enzymes use the same chemical groups as small molecule catalysts; and ii) investigation of RNase A to address the catalytic contribution from interconnected catalytic strategies.



a biomolecule
logo of Dr Sorin's website


Eric Sorin's research group applies computational tools to examine the structure, stability, and dynamics of biological molecules of varying sizes and chemical compositions. Specific topics being studied in this lab include protein and RNA folding and misfolding, the development of accurate all-atom models for lipid membrane simulation, and enzyme-inhibitor interactions relevant to drug design. They apply a variety of models and methods, with a focus on Molecular Dynamics, and utilize the Folding@Home Distributed Computing resource to sample large numbers (tens of thousands) of independent simulations. These tools have allowed them to examine fundamental protein and RNA folding processes in detail, and to assess the effects of bulk ensemble averaging on the kinetics and mechanisms of interest, thus bridging the gap between single-molecule and bulk experimental measurements. This massive computational power allows them to examine differences that may arise based on changes in the molecular system being studied, the model being employed, and the environmental conditions being modeled.



system design schematic



Hadi Tavassol's research group focuses on fundamental understanding and design of chemical interfaces, especially in electrochemical systems. The group fabricates materials, specifically designed toward interfacial processes, which are essential in the system level performance of electrochemical devices, and mimic biological systems. Students in the group use in-situ characterization techniques to elucidate the interplay of materials and function. Tavassol group members prepare inter-layers, thin films, and molecular assemblies and employ advanced electrochemical and laser spectroscopy techniques to study energy devices and biological systems.






helical structure of a biomolecule


Paul Weers' research group is focused on the understanding of the structure-function relationship of exchangeable apolipoproteins, which are critical proteins responsible for the transport of lipids. They use a combination of protein biochemistry, molecular biology and biophysics to address questions related to the ability of the protein to interact with hydrophobic materials. Invertebrate apolipophorin III, for which high resolution structures are available, is used as a model to investigate apolipoprotein-lipid interactions at the molecular level. The group also studies the role of apolipoproteins in innate immunity, e.g. their ability to neutralize lipopolysaccharides, the toxic membrane components of Gram negative bacteria and responsible for sepsis.