Research and Teaching Interests
 In the broadest sense, our research objectives are to understand how proteins function in biological systems. Our interests range from understanding how energy is converted in photosynthetic systems to how changes in proteins can cause certain diseases. We use a variety of biochemical and biophysical approaches to examine each problem, with an emphasis on relating the functional properties to the structure. Therefore, one major aspect of our research is the determination of the three-dimensional structures of proteins by x-ray crystallography.
One major focus is the photosynthetic process, the conversion of light energy into chemical energy that involves a variety of pigment-protein complexes. Our research goal is to develop models for the transfer of electrons and energy in these complexes, in particular to understand how these processes changed as primitive bacteria evolved into cyanobacteria and plants. To achieve this goal, we create bacterial complexes with new cofactors that resemble those cofactors found in the corresponding plant proteins. We are also interested in understanding how the light energy is used to drive various metabolic processes, specifically how nitrogen in assimilated in organisms.
The influence of proteins on medical problems is also studied in our laboratory. Nicotine interacts with the human body through a protein called the nicotinic acetylcholine receptor. For this receptor, structural studies are underway to develop a molecular understanding of how this protein functions with a long-term goal of developing therapies for addiction. When introduced in the cell, certain proteins can recognize features of specific cell types. The mechanism by which toxins use this ability to target a narrow range of organisms is being studied with a goal of developing new means of using these toxins against disease carrying insects such as mosquitoes.
|
| Representative Publications
"X-ray crystallography of photosynthetic proteins, in Biophysical techniques in photosynthesis," P. Fromme and J. P. Allen , Advances in Photosynthesis and Respiration, Springer Publishers , in press (2008).
"Protein dynamics control the kinetics of initial electron transfer in photosynthesis," H. Wang, S. Lin, J. P. Allen, J. C. Williams, and N. Woodbury , Science 316, 747-750 (2007).
"Changes in metal specificity due to iron ligand substitutions in reaction centers from Rhodobacter sphaeroides," J. C. Williams, M. L. Paddock, Y. P. Way, and J. P. Allen , Applied Magnetic Resonance 31, 45-58 (2007).
"Structural insights into the evolution of a non-biological protein: importance of surface residues in protein fold optimization," M. D. Smith, M. A. Rosenow, M. Wang, J. P. Allen, J. W. Szostak, and J. C. Chaput , Plos One 5, 1-11 (2007).
"The structure of phenoxazione synthase from Stretomyces antibioticus reveals a new type 1 copper center," A. W. Smith, A. Camara-Artigas, J. P. Allen and W. Francisco , Bochemistry 45, 4378-4387 (2006).
"Design of a redox-linked active metal site: manganese bound to bacterial reaction centers at a site resembling that of photosystem II," M. Thielges, G. Uyeda, A. Camara-Artigas, L. Kalman, J.C. Williams and J.P. Allen, Biochemistry 44, 7389-7394 (2005).
"Structure of spinach nitrite reductase: implications for multi-electron reactions by the iron-sulfur:siroheme cofactor," U. Swamy, M. Wang, J. N. Tripathy, S. H. Kim, M. Hirasawa, D. B. Knaff, and J. P. Allen , Biochemistry 44, 16054-16063 (2005).
"Proton release due to manganese binding and oxidation in modified bacterial reaction centers," L. Kalman, M. Thielges, J. C. Williams, and J. P. Allen , Biochemistry 44, 1266-1273 (2005).
|
