Elisar Barbar

The Barbar lab focuses on elucidating molecular processes that govern protein networks involving intrinsically disordered proteins (IDPs). Our approach includes characterization of protein assemblies using combined analysis from multiple biophysical techniques. We obtain structural information by NMR, crystallography, and negative stain electron microscopy, binding thermodynamics by isothermal titration calorimetry (ITC), hydrodynamics by size exclusion chromatography multiangle light scattering (SEC-MALS) and analytical ultracentrifugation (AUC), and dynamics by NMR. Current projects focus on the intermediate chain of cytoplasmic dynein, viral proteins (Rabies, COVID, HPIV, Ebola), the transcription factor ASCIZ, a tumor suppressor 53BP1, and other partners of the hub protein LC8.

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Afua Nyarko

The Nyarko lab investigates mechanisms of multivalent protein assemblies in signaling pathways, with the goal of identifying novel strategies to selectively modulate downstream responses. Our primary focus is the Hippo signaling pathway, a network of protein-protein associations critical to the homeostatic balance of cell growth versus cell death. We combine a variety of mutually reinforcing molecular biophysics methodologies including solution NMR to advance understanding of the fundamental mechanisms of protein associations in the Hippo signaling pathway, elucidate the regulatory importance of multivalent intrinsically disordered proteins in the signaling network, and decipher the strong link between Hippo signaling dysregulation and cancer.

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Juan M. Vanegas

The Vanegas laboratory combines techniques from molecular simulation, continuum mechanics, and quantum chemistry to understand how molecular structure modulates the activation of mechanosensitive proteins and determines the mechanical response of lipid membranes. His group is highly interdisciplinary working at the interface between biology, physics, chemistry, and engineering. The central focus of our research is to provide mechanistic insights into essential biological processes such as membrane fission and fusion, organelle and cellular shaping, touch and pain sensing, cardiovascular control and development, and osmotic regulation among others. He works closely with other laboratories to integrate our modeling efforts with experimental results.

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David Hendrix

The Hendrix lab has organized the largest meta-database of RNA secondary structures. This database has enabled the analysis of secondary structure, including uncovering patterns associated with specific structures, balance of thermodynamic energy, and in the development of new structural alignment methods. We have also developed several approaches including machine learning and deep learning to microRNA discovery and analysis of microRNA biogenesis.

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Colin Johnson

The Johnson lab studies the role of membrane proteins in Ca2+ signaling and disease. Through development of new organismal models for in vivo study of pathological mutations, and reconstitution of the signaling steps in an in vitro setting, we have identified key proteins that link rises in intracellular Ca2+ with physiological processes and dysfunction including hearing, deafness, cell membrane repair, and muscular dystrophy. Our long-term goals are both to improve our basic understanding of the signaling associated with these processes, and the development of potential therapeutics.

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Rick Cooley

The Cooley lab seeks to understand how phosphorylation regulates protein structure and function to coordinate cellular signaling events, with the ultimate goal of discovering novel strategies by which specific phosphorylated forms of proteins can be targeted for therapeutic intervention. Using a combination of Genetic Code Expansion and a variety of biophysical techniques including x-ray crystallography, small angle x-ray scattering and NMR, we focus on i) uncovering mechanisms by which 14-3-3 regulates phospho-protein function and ii) how phosphorylation alters protein-protein interactions in apoptotic pathways.

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Patrick Reardon

Dr. Reardon directs the OSU NMR Facility and conducts research focused on using NMR to study complex biological problems. We are developing In-Cell NMR tools to enable atomic resolution structural and dynamic analysis of proteins in living cells. We also develop NMR methods to measure stable isotope labeling in metabolites and utilize this information to map metabolic fluxes in biological systems. Dr. Reardon operates the analytical ultracentrifuge and collaborates with a number of groups to characterize macromolecules and their complexes.

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Weihong Qiu

The Qiu lab seeks to understand the interplay between kinesin-5 and kinesin-14 motor proteins in bipolar spindle assembly using an interdisciplinary approach that integrates molecular biology, protein biochemistry, cell biology, structural biology, physics-based theoretical modeling, and single-molecule light microscopy.

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Andy Karplus*

Dr. Karplus no longer leads a research group but still is involved in collaborative work with others who study proteins. Proteins play central roles in all aspects of biochemistry and detailed structural information is a key ingredient to understanding the mechanisms involved in protein function. One main expertise Karplus brings is in solving detailed protein structures by X-ray crystallography, and in interpreting those structures in light of functional and evolutionary information to figure out how they work.

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Victor Hsu

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