Joanna R. Long, Ph.D.
Associate Professor
Biochemistry and Molecular Biology
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Joanna R. Long, Ph.D. |
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Protein structure and dynamics in heterogeneous environments Our research focuses on the relationship between proteins and their environment in mediating the properties of specialized tissues. In structural biology, a central tenet is the 3D structures of proteins are dictated by their primary amino acid sequences; once you understand how a particular protein folds based on this sequence, you will be able to predict its functional properties. While this is an attractive paradigm, in condensed, heterogeneous environments, such as lipid membranes and extracellular matrices, a multifaceted relationship between protein sequence, the surrounding environment, structure, and dynamics exists. Solid state NMR (ssNMR) has emerged as a technique that is uniquely capable of obtaining high resolution data without placing strict constraints on the physical state of the protein. My lab uses a combination of standard biophysical assays, functional assays (in collaboration with other research groups at UF), and state-of-the-art ssNMR experiments to address three medically relevant problems: 1) Membrane-associated proteins determine the unique physical properties of pulmonary surfactant, yet little is known about their atomic-level structure and dynamics in the membrane environment. We currently are funded by the NIH to study the structure and dynamics of lung surfactant peptides interacting with lipids found in the lung. 2) Transmembrane peptide helices transduce signals across cell membranes, yet little is known about the role membrane composition plays in their performance. Our work is currently focused on the ion channel-forming M2 segments of the nicotinic acetylcholine receptor (nAChR) to yield insights into key features of aging-related changes in membrane composition that affect the function and regulation of ion channel gating. This research is currently funded by the American Heart Association. 3) Osteoblasts secrete extracellular proteins including type I collagen and the anionic phosphoprotein bone sialoprotein II (BSP); BSP is thought to be critical to nucleation of hydroxyapatite (HAP) in mineralization of the collagen matrix during the formation of bone. We are studying the molecular level interactions of BSP with HAP and collagen and the regulation of BSP function through phosphorylation.
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Status: Possibly Accepting New Students This Year Contact Information: office: MBI LG-126 lab: MBI LG-129 phone: 352-846-1506 email: jrlong@mbi.ufl.edu Home Page Biography: Joanna R. Long received her Ph.D. in Physical Chemistry from the Massachusetts Institute of Technology in 1997 for work done in the laboratory of Prof. R. G. Griffin on applying solid state NMR techniques to the study of peptide and lipid structure and dynamics. She then joined the laboratory of Prof. Pat Stayton in the Department of Bioengineering at the University of Washington, in collaboration with Prof. Gary Drobny, to do postdoctoral research studying protein structure and dynamics at mineral and polymer interfaces for tissue engineering applications. In 2000, she joined the Department of Chemistry at the University of Washington as Director of the NMR Facility. She joined the Faculty at the University of Florida in 2002. |
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