Johann Deisenhofer is currently Professor Emeritus at the UT Southwestern Medical Center in Dallas, Texas. Until January 2019 he held the positions of Regental Professor, Professor in Biophysics, and Virginia and Edward Linthicum Distinguished Chair in Biomolecular Science at UT Southwestern. Between 1988 and 2010 he also was an Investigator in the Howard Hughes Medical Institute. Born in Germany in 1943, Deisenhofer studied physics at the Technical University Munich, and received a doctoral degree in experimental physics in 1974. He worked in the Department of Structural Research, led by Robert Huber, at the Max-Planck-Institute for Biochemistry in Martinsried near Munich, until in 1988 he moved to Dallas. The main research interest of the Deisenhofer laboratory since 1988 has been the structural biology of integral membrane proteins, proteins involved in light signaling and energy conversion, proteins involved in immunity, and proteins involved in cholesterol homeostasis. For the determination of the three-dimensional structure of a bacterial photosynthetic reaction center, Deisenhofer received the 1986 Biological Physics Prize of the American Physical Society (with Hartmut Michel), the 1988 Otto-Bayer-Prize (with Hartmut Michel), and the 1988 Nobel Prize in Chemistry (with Hartmut Michel and Robert Huber).

Research Interests

We study the three-dimensional structures of biological macromolecules with the methods of x-ray crystallography. Our results enhance our understanding of the function and the structural stability of these molecules; they extend the database of known structures, which has become a most valuable resource for biomedical research. Among the techniques we use are heterologous expression, purification, crystallization, and mutagenesis of proteins, x-ray diffraction, computational crystallography, and structure analysis. Our interests focus on the following main areas: proteins involved in energy transfer and electron transfer, proteins using light energy, membrane proteins, membrane associating proteins, chaperonins, and proteins with repeating sequence motifs. Among the structures we determined during the last ten years are two cytochromes P450, the adenovirus type 5 knob protein, porcine ribonuclease inhibitor and its complex with bovine ribonuclease A, DNA photolyase and GroES from E. coli, gp31 (a viral homolog of GroES), human cpn10, SecA protein, the murine MHC Class I molecule H2-M3, the C-domain of bovine synapsin I, and the cytochrome bc1 complex from bovine heart mitochondria.

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Section 29: Biophysics and Computational Biology