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The University of Tennessee, Knoxville

Views of Structure and Function at the Nanoscale

Cynthia Peterson, ProfessorCollege of Arts and Sciences - Department of Biochemical, Cell & Molecular Biology

Biological molecules are the engines that control life. Biochemistry has evolved to study just how that happens. Researchers are interested in the way our bodies fight injury and battle disease during clot formation and wound healing, the inflammatory response and cancer. In particular, our laboratory focuses on the structure and function of plasminogen activator inhibitor-1 (PAI-1), the main regulator of blood clot lysis. We are unraveling the role of other proteins/cofactors in regulating PAI-1 activity. If left unregulated, PAI-1 would lead to bleeding disorders and inappropriate activities in tissues throughout the body. How do we tackle these problems? State-of-the art structural and computational tools are employed to address PAI-1 binding with its cofactors to understand the way that intimate details of protein shape guide molecular recognition. We cannot see PAI-1 or its cofactors, even with the most powerful microscopes. Instead, we use varied biological “lenses” to visualize these biomolecules and understand their size, shape and multiple interactions. With these approaches, we reconstruct a picture of what is happening on the nanoscale. Our recent work harnesses the power of neutrons to study biomolecules, working closely with colleagues at ORNL at the High Flux Isotope Reactor. This neutron scattering research is a means to tackle one of the most challenging areas left for structural biologists, which ironically is finding experiments to characterize intrinsically unstructured regions in proteins! Our work reveals that unstructured regions in the cofactors are some of the most important in regulating PAI-1.​

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