Featured Research Toxic fibrillar oligomers of amyloid-ß have cross-ß structure — Prof. David S. Eisenberg The neurodegenerative diseases and Amyloid structure
Professor Eisenberg investigates the structure of toxic fibrillar oligonmers of amyloid-ß.
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Several of our research groups focus on the areas of Structural and Computational Biology.
X-ray crystallography, NMR, EPR, and other biophysical techniques are being brought to bear on exciting new problems in biology through the elucidation of the functions and cellular mechanisms of diverse proteins, nucleic acids, macromolecular assemblies, and disease-related molecules.
Studies aimed at elucidating biological phenomena are supported by technical developments aimed at advancing the current limits of structural biology methods. Our structurally-oriented research programs are strongly complimented by diverse studies in computational and synthetic biology. These range from algorithmic developments in the areas of bioinformatics and genomics to macromolecular structure prediction and design.
Professor James U. Bowie are fascinated by protein structure, folding and stabilization. This interest has led them into three main areas: (1) learning how membrane proteins fold and how they can be stabilized; (2) the structures and biological functions of a biological polymer they discovered, that is formed by a very common protein module called a SAM domain; (3) developing and stabilizing enzyme pathways for the production of biofuels. Professor James Bowie and his group Professor Robert T. Clubb investigates the molecular basis of bacterial pathogenesis. In particular, his group studies how microbes display and assemble cell wall attached surface proteins, and how they acquire essential nutrients from their host during infections. The group's study could lead to creating new inhibitors of bacterial infections. Professor Robert Clubb Professor David S. Eisenberg focus on protein interactions. In their experiments they study the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state. In bioinformatic work, they derive information on protein interactions from genomic and proteomic data, and design inhibitors of amyloid toxicity. Professor David Eisenberg and his research group Professor Juli Feigon study nucleic acid structure and specific recognition of nucleic acids by proteins. Her group focuses on determining the three-dimensional structures of DNA and RNA, and on investigating their interactions with various proteins and ligands, and to study nucleic acid folding. Professor Juli Feigon and her research group Professor Wayne L. Hubbell Dr. Hubbell's research is focused on understanding the relationship between the molecular structure of a protein and the conformational changes that control its function. Of particular interest are membrane proteins that behave as "molecular switches", i.e., proteins whose structures are switched to an active state by a physical or chemical signal. Professor Christopher J. Lee Professor Christopher Lee's main area of research is in bioinformatics. His group studies 1) analysis of alternative splicing and genome evolution, 2) analysis of protein evolutionary pathways, and 3) development of a general framework for working with genomic data as an abstract graph database. Professor Joseph A. Loo The research interests of Professor Loo's group include the development and application of bioanalytical methods for the structural characterization of proteins and post-translational modifications, proteomics-based research, and the elucidation of of disease. The composition and structure of noncovalently-bound protein-protein and protein-ligand interactions are studied by electrospray ionization mass spectrometry and ion mobility. Professor Margot E. Quinlan use biochemistry, microscopy and genetic approaches to study regulation of the actin cytoskeleton. The group is currently focused on Spire (Spir) and Cappuccino (Capu), two proteins that collaborate to build an actin network essential for early body axis development. Combining an in vitro understanding of the mechanism of Spir and Capu with in vivo studies of polar cells will provide insight into how the actin cytoskeleton is regulated and a broader understanding of cell polarity. Professor Margot Quinlan and her group Professor Emil Reisler Professor Emil Reisler and his group investigate cell motility and force generation mechanism of actin, tubulin, and a family of motor proteins. The aim of these studies is to obtain a structural description of the mechanism of motion and force generation. At the cellular level, the group studies the function, interactions, and structural transitions of the assembled protein systems. Professor Jose Rodriguez studies the complex architecture of biological systems - from single biomolecules to cellular assemblies - at high resolution. His work is largely based on diffraction phenomena and combines computational, biochemical and biophysical experiments. The development of new methods is central to this work, particularly using emerging technologies in cryo-electron microscopy, nano and coherent x-ray diffraction, and macromolecular design. Combined, these tools can reveal undiscovered structures that broadly influence chemistry, biology, and medicine. Prof. Rodriguez Professor Todd O. Yeates focus heavily on structural, computational, and synthetic biology aspects of chemistry. The group's emphasis is on supra-molecular protein assemblies and synthetically designed protein assemblies, and conducts research in computational genomics in order to infer protein function and to learn new cell biology. Dr. Todd Yeates and his group