John J. Tanner
Protein crystallography; molecular dynamics simulation; protein structure and dynamics; molecular recognition; enzymology.
- BS, University of Missouri-Columbia, 1983
- PhD, Brown University, 1988
- Professor, University of Missouri-Columbia, 2006-present
- Associate Professor, University of Missouri-Columbia, 2002-2006
- Assistant Professor, University of Missouri-Columbia, 1997-2002
- Postdoctoral Associate, University of Houston (Biochemistry), 1991-1997
- Postdoctoral Associate, University of Houston (Chemistry), 1988-1991
My group is studying the interplay among the form, flexibility, and function of biological molecules, with a particular interest in understanding how biomolecules recognize and engage one another. Biomolecular recognition is important because virtually all of biological chemistry occurs when two or more molecules come together to effect a reaction or to transmit a signal. For example, enzymes must discriminate their natural substrates from the myriad of other molecules in living cells, while the recognition of foreign molecules by antibodies is the basis of our immune system.
We study biomolecular recognition using both experimental and computational tools. Our major experimental technique is X-ray crystallography, which provides high resolution images of biological molecules such as proteins and nucleic acids. On the computational side, we rely on molecular dynamics simulations and data base mining. Computer simulations provide information about molecular motion and flexibility that is not readily obtainable from crystallography. Mining of the vast data base of three-dimensional protein structures is used to identify correlations between protein structure and function. This combination of experiment and computation provides unique insights into how biological molecules carry out the chemistry of life. Ongoing projects include high resolution crystallographic studies of the enzymes such as D-glyceraldehyde-3-phosphate dehydrogenase and proline dehydrogenase, crystallography and simulations of antibodies engaged with DNA, and studies of enzyme recognition of nicotinamide adenine dinucleotide (NAD).
Crystals of proteins under study in the Tanner group
Crystal structure of GAPDH from T. aquaticus (left)
and a closeup view of the bound NAD (right)
Snapshots from a computer simulation of NAD in water
Please see my group website for a complete list of publications.