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 BIOGRAPHY |
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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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RESEARCH DESCRIPTION |
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Proteins and peptides found at biological interfaces play key roles in regulating processes ranging from bone formation and remodeling to cell signaling to expansion and compression in the lungs. Understanding the roles protein and peptide structure and dynamics play in these complex environments is of critical importance for regulating cellular differentiation, understanding disease pathologies, and designing therapeutic strategies. The ability to elucidate biomolecular structure and dyanamics in heterogeneous systems under In situ conditions makes solid state NMR uniquely suitable for studying these systems. Ongoing projects include: 1) the role of lung surfactant proteins and synthetic analogs in regulating membrane biophysics, 2) Amyloid b-peptide structure and dynamics in various states of aggregation and association with membranes, 3) examining structure/function relationships in the regulation of hydroxyapatite mineralization by bone sialoprotein. |
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