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Rodney Biltonen, Ph.D. Emeritus Professor of Pharmacology and Biochemistry Publications | Laboratory | NIH Biosketch (PDF) |
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Thermodynamics and Kinetic Basis of Regulation of Interacting Biological System The general objective of my laboratory is to thermodynamically and kinetically characterize interacting systems of biological relevance, and to understand quantitatively the overall basis of the mechanism of action of such systems and their modulation. In the past, we have studied the nature of protein unfolding, ligand interactions of ribonuclease A, the thermodynamic of structural changes in tRNA, and the thermodynamic and kinetic basis of the substrate supply cycle during protein synthesis. Our current interest is the role of membrane structural fluctuations in modulation of membrane function, particularly its role in the activation of phospholipases and other peripherally-bound proteins. In these studies, several experimental approaches including titration and scanning calorimetry, fluorescence spectroscopy, Fourier transform infrared spectroscopy and nuclear magnetic resonance spectroscopy are used. In some cases, new instrumentation is developed. For example, we have designed and constructed a high-sensitivity differential canning calorimeter, a temperature scanning pH-stat and in collaboration with Dr. M.L. Johnson, a dynamic calorimeter which can monitor the kinetics of membrane phase transitions. Our laboratory continues to be involved with theoretical approaches to better understand these systems. For example, we are developing Monte-Carlo approaches to help answer the question of compositional distribution in mixed bilayer systems. Computers play important roles in all aspects of our work, including computer control of instruments, data acquisition, mathematical modeling and process simulation. Funding for this research has been provided by grants from the National Institutes of Health and the National Science Foundation. |