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 a new Mn cofactor that resembles the site of water oxidation in cyanobacteria and plants.
The influence of proteins on medical problems is also studied in our laboratory. The major leading genetic cause of childhood deaths is SMA, spinal muscular atrophy, in which neurological systems fail to properly develop. The cause of this disease is a change in the protein SMN, for survival of motor neurons. To determine the molecular reasons for why changes in the SMN protein give rise to SMA, we are investigating the three-dimensional structures of the SMN protein found in both healthy and SMA patients.
"Light-driven oxygen production from superoxide by Mn-binding bacterial reaction centers," J. P. Allen, T. L. Olson, P. Oyala, W.-J. Lee, A. Tufts, and J. C. Williams , Proc. Natl. Acad. Sci. USA 109 2314-2318 (2012)
"Reinterpretation of the electron density at the site of the eighth bacteriochlorophyll in the FMO protein from Pelodictyon phaeum," D. Tronrud and J. P. Allen , Photosynthesis Research 112 71-74 (2012)
"pH dependent structural conformations of B-phycoerythrin from Porphyridium cruentum," A. Camara-Artigas, M. Andujar-Sanchez, E. Ortiz-Salmeron, J. Bacarizo, C. Mesa-Valle, C. Cuadri, J. M. Martin-Garcia, T. M. Sobcuk, J. Ibanez and J. P. Allen , FEBS Journal 279 3680-3691 (2012)
"Carotenoid excited state properties in photosynthetic purple bacterial reaction centers: Effects of the protein environment," J. Pan, S. Lin, J. P. Allen, J. C. Williams, H. A. Frank, and N. W. Woodbury , J. Phys. Chem. B 115 7058-7068 (2011)
"Thin film voltammetry of wild type and mutant reaction center proteins from photosynthetic bacteria," Y. Zhang, A. M. LaFountain, N. Magdaong, M. Fuciman, J. P. Allen, H. A. Frank, and J. F. Rusling , J. Phys. Chem. B 115 3226-3232 (2011)