Charles Brooks The Brooks group is engaged in research that centers around the theoretical and computational description of proteins, nucleic acids and their complexes. These efforts include ongoing research problems in protein folding; multi-scale modeling of macromolecular motors (e.g., ribosomes, helicases); protein-ligand interactions and drug discovery/design (docking, free energy perturbation methods); viral capsid assembly, energetics and conformational transitions; large-scale conformational transitions in biological macromolecules; ion channel transport and selectivity mechanisms; membrane protein insertion, folding and assembly; GPCR and other integral membrane protein modeling and dynamics. [Chemistry, Biophysics, PIBS, Bioinformatics]
Heather Carlson Our studies broadly focus on the molecular recognition between ligands and proteins, from the fundamental biophysics of ligand binding to applied inhibitor design. Major focii in the lab are understanding protein flexibility/dynamics/allostery, incorporating those phenomena into structure-based drug design, and large-scale mining of protein structures to discover fundamental properties of binding sites. [Medicinal Chemistry, Biophysics, Bioinformatics, Chemistry]
Gordon Crippen Our work consists of devising new algorithms to solve problems associated with protein structure and creating the computer programs that use these algorithms to analyze experimental results and make new predictions. [Medicinal Chemistry, Biophysics, Bioinformatics]
Ming Lei The goal of our laboratory is to understand the organization and dynamics of macromolecular assemblies important for genome regulation and stability. A combination of structural analyses, such as X-ray crystallography and electron microscopy, coupled with biophysical and biochemical experimentation, forms the core of our methodological approach. [PIBS, Chemical Biology, Biophysics]
A. Ramamoorthy We are investigating the structure, dynamics and function of membrane-associated cytochrome b5 and P450 proteins using NMR spectroscopy. The structural interactions between these two proteins are being investigated at atomic-resolution using solid-state NMR techniques. [Biophysics, Chemistry, PIBS]
Gabby Rudenko Our laboratory uses structural biology, biochemical and biophysical techniques to study a number of proteins involved in: (1) formation and maintenance of synapses and (2) response to psychoactive compounds. [PIBS]
Mark Saper The Saper lab studies the molecular mechanisms of how pathogenic bacteria produce and secrete a large capsule polysaccharide that enhances bacterial virulence. In particular, lab members study the structure and function of proteins that produce the group 4 capsule of two pathogenic E. coli strains with both biochemical and crystallographic techniques. Current projects address why reversible tyrosine phosphorylation by a kinase and phosphatase is essential for the secretion process. [PIBS, Biophysics, Chemical Biology]
Yiorgo Skiniotis The Skiniotis group is employing molecular electron microscopy techniques to study the architecture and conformational dynamics of complex protein assemblies, aiming to address mechanistic issues in the related biological processes. Our current focus is on the structural characterization of chromatin remodeling complexes and signaling cell surface receptors. [PIBS]
Janet Smith The Smith lab studies the molecular mechanisms of proteins primarily by using X-ray crystallography to determine three-dimensional structures. Most of our projects are structure-function studies of complex enzymes, in which several enzyme domains work together to catalyze multi-step reactions. Currently we are studying polyketide synthases, replication enzymes of RNA viruses, and glutamine amidotransferases. [PIBS, Biophysics, Chemical Biology]
Jeanne Stuckey The Stuckey laboratory has an active research program using structure-based drug design to develop new cancer therapies. In addition, we are interested in studying the structure-function relationship of membrane modifying enzymes that are involved in a variety of diseases such as cancer, diabetes and neuropathies. [PIBS]
John Tesmer We use the technique of X-ray crystallography to study the molecular basis of G protein-coupled receptor-mediated signal transduction. By determining the structures of signaling proteins alone and in complex with their various targets, we can provide important insights into the molecular basis of signal transduction and the disease states that emerge as a result of dysfunctional regulation of these pathways. [PIBS, Biophysics, Chemical Biology]
Oleg Tsodikov We perform structural and functional studies of proteins involved in DNA replication and repair in Mycobacterium tuberculosis. These vital cellular processes are excellent drug targets. We are working towards rational structure-driven discovery of efficient DNA replication inhibitors in mycobacteria that can serve as new anti-tubercular drugs. Our group is also studying other biological systems in collaboration with different laboratories on and off the UM campus. We use the two-prong approach of X-ray crystallography and biophysical solution studies. [Medicinal Chemistry, Chemical Biology]
Raymond Trievel Our laboratory is interested in understanding the molecular basis by which proteins are post-translationally modified and how these modifications impact biological functions. Toward this goal, we are utilizing both structural and biochemical techniques to elucidate the mechanisms and specificities of enzymes that catalyze covalent modifications, such as protein methyltransferases and acetyltransferases. We are particularly interested in enzymes that catalyze histone modifications, which have been implicated in epigenetic gene regulation and cancer. [PIBS, Biophysics, Chemical Biology, CMB]
Zhaohui Xu We focus on understanding the molecular mechanism underlying membrane trafficking in the cell, with a keen interest in the structure and function of proteins involved in the process. Our primary research tool is high-resolution X-ray crystallography. [PIBS, Biophysics, Chemical Biology, CMB]
Matthew Young Our laboratory focuses on the structure-function relationships that help regulate the activities of cell signaling proteins, currently protein kinases and nuclear receptors. We are particularly interested in the molecular motions of these proteins and the conformational transitions that these proteins undergo as part of their regulatory mechanisms. [PIBS, Bioinformatics, Biophysics]
Erik Zuiderweg NMR studies of protein conformation and dynamics in solution, concentrating on allosterics in the Hsp-70 chaperone proteins. [PIBS, Biophysics, Chemistry, Chemical Biology]
