John Wise


Associate Professor

Biological Sciences


Office: DLSB 332
Phone: 214-768-3426
Email: jwise[@]

Educational Background

Ph.D. University of Rochester


Lab: DLSB 332
Tel: 214-768-1789


My Science Webpage can be found here

Public Lectures A lecture on the Evolution of Cancer and problems in Chemotherapy: “Down in the Trenches - Gene Families and their Effects on Modern Medicine"

A lecture on Intelligent Design for “The Scientific Method – Critical and Creative Thinking” at the Department of Physics at SMU "Intelligent design is not science"

Research Interests

Multiple Drug Resistance Proteins
  • Structural studies
  • Drug Transport Mechanism studies
  • Small molecule drug docking
  • Virtual screening technologies for new inhibitors
Rotary Motors from Biology and ATP Synthase Research
  • Enzymatic mechanism studies
  • Mechanisms of multisite cooperative catalysis
  • Mechanisms of ligand binding in complex multisubunit systems
  • Membrane protein complex ion-pumping mechanisms in coupled membrane systems
Combinatorial Biology and the Evolution of DNA Binding Proteins
  • Design and construction of combinatorial mutagenesis systems for altering DNA binding protein sequence specificity
  • Design and optimization of in vivo reporter assays for screening combinatorial DNA binding protein variants for altered specificities and affinities
  • Applications of combinatorial approaches to determining specific protein-DNA recognition and binding mechanisms
Toxins and Toxic Genes for Selection Systems and Therapies
  • Use of antigen-ribosomal toxin fusions for therapy development in autoimmune disease (a Myasthenia gravis model)
  • Toxic-gene expression systems and suppressor-based toxin expression for in vivo selection applications
  • Chemical synthesis of novel, metabolic "pre-toxins" activated by beta-galactosidase
In silico Simulation and Modeling of Protein and Small Molecule Structures

Modern computational methods give novel insight into the structure and function of proteins and enzymes. Two examples of visual output from these computational methods are given below.


Left Panel:A short model peptide modified at a cysteine residue with a stable free radical nitroxide probe. Protein modifications such as this one allow the determination of the details of a protein's structure and function.

Right Panel:Another modeled free radical spin probe. The peptide backbone is shown as a purple line. The residue is shown in colors coded for each atom type (Dark Blue = nitrogen, Light Blue = carbon, Red = oxygen, White = Hydrogen, Yellow = sulfur).


Left Panel:Model of a transcriptional control protein bound to its specific DNA binding sequence. Protein DNA interactions like this are the common starting point for the control of gene expression. This structure of the 434 Cro protein complexed with a 20 base pair piece of DNA containing its Operator OR1 was determined by A.Mondragon & S.C.Harrison (protein data bank accession code 3cro). The secondary structure of the protein is shown schematically in gray; the DNA double strands are shown in colors coded for each atom type (see left panel - Orange= phosphorous).

Right Panel:Model of a multidrug resistance pump from humans showing a steric conflict between a substrate and a drug. These proteins are important in cancer and viral chemotherapies. The purple rods and yellow ribbons show the enzyme and the drug and substrate molecules are shown with van der Waal's spheres.

Selected Publications

Hornung, T., Volkov, O., Zaida, T.M.A., Delannoy, S., Wise, J., and Vogel, P.D. “Structure of the Cytosolic Part of the Subunit b-Dimer of Escherichia coli FoF1-ATP Synthase” (2008) Biophys. J. 94, 5053-5064

Wise, J.G. and Vogel, P.D. “Subunit b dimer of the Escherichia coli ATP synthase can form left-handed coiled coils” (2008) Biophysical J. 94, 5040-5052

Hossann, M., Li, Z., Shi, Y., Kreilinger, U., Blattner, J., Vogel, P.D., Yuan, J.M., Wise, J.G., Trommer, W.E. (2006) “Novel Immunotoxin: A Fusion Protein Consisting of Gelonin and an Acetylcholine Receptor Fragment as a Potential Immunotherapeutic Agent for the Treatment of Myasthenia Gravis”, Protein Expression and Purification46, 73-84.

Motz C, Hornung T, Kersten M, McLachlin DT, Dunn SD, Wise JG, Vogel PD (2004) “The subunit b dimer of the FoF1-ATP synthase: Interaction with F1-ATPase as deduced by site-specific spin-labeling”, J. Biol. Chem. 279, 49074-81.

Guo, C., Li, Z., Shi, Y., Xu, M., Wise, J.G., Trommer, W.E., Yuan, J. (2004) “Intein-mediated fusion expression, high efficiency refolding and one-step purification of gelonin toxin”, Protein Expression and Purification 37, 361-367.

Fromknecht, K., Vogel, P. and Wise, J.G. (2003) “Combinatorial Redesign of the DNA Binding Specificity of a Procaryotic Helix-Turn-Helix Repressor”, J. Bacteriology 185, 475-81

Guhr, P., Neuhofen, S., Coan, C., Wise, J.G., and Vogel, P.D., (2002) “New Aspects on the Mechanism of GroEL-Assisted Protein Folding”, Biochim. Biophys. Acta 1596, 326-335

Chelius, D., Loeb-Hennard, C., Fleischer, S., McIntyre, J.O., Marks, A.R., De, S., Hahn, S., Jehl, M.M., Moeller, J., Philipp, R., Wise, J.G. & Trommer, W.E. (2000) “Phosphatidylcholine activation of human heart (R)-3-hydroxybutyrate dehydrogenase mutants lacking active center sulfhydryls: Site-directed mutagenesis of a new recombinant fusion protein”, Biochemistry 39, 9687-9697.

Kersten, M.V., Dunn, S.D., Wise, J.G., and Vogel, P.D. “Site-Directed Spin-Labeling of the Catalytic Sites Yields Insight into the Structure of the Fo F1-ATP Synthase of Escherichia coli”, (2000) Biochemistry 39, 3856-3860.

Vogel, P.D. and Wise J.G. “Studienbrief Technik in der Medizin: Gentechnische Arbeitsmethoden”, (1999) Zentrum für Fernstudien & Universitäre Weiterbildung, Universität Kaiserslautern

Loesel, R.M., Wise, J.G. and Vogel, P.D. (1997) “Asymmetry in Catalytic Sites but not in Noncatalytic Sites in the Escherichia coli F1-ATPase”, Biochemistry 36, 1188-1193

Schanding, T., Vogel, P.D., Trommer, W.E. and Wise, J.G. (1996) “Synthesis of a pH-Sensitive Spin-Labeled Cyclohexylcarbodiimide Derivative for Probing Protonation Reactions in Proton-Pumping Enzymes”, Tetrahedron 52, 5783-5792

Articles on Evolution and the Value of Science written or co-authored by me

From the Dallas MORNING NEWS:

"Speaking out against intelligent design" April 5, 2007

From the SMU DAILY CAMPUS newspaper:

"Intelligent Design is not science: why this matters" May 4, 2007

"ID claims don't hold up" April 26, 2007

"Letter to the Editor - Deceptive Tactics from the Discovery Institute" April 25, 2007

"Letter to the Editor - A Response to Levy and Smith" April 12, 2007

"Intelligent design isn't intelligent" February 11, 2005


Syracuse University B.S. 1977 Biology magna cum laude
University of Rochester M.S. 1980 Biochemistry
University of Rochester Ph.D. 1983 Biochemistry

Courses I Presently Teach at SMU

  • Introduction to Biology (BIOL 1401)

    4 semester hours, Fall semester

    A first semester course in introduction to biology, intended for undergraduate biology majors. The course covers basic chemistry and thermodynamics, macromolecules, metabolism, cell structure and function, membranes, respiration and photosynthesis, cellular communication, cell cycle, mitosis, meiosis, chromosomal inheritance, replication, transcription and translation, microbial and eukaryotic genomes and DNA technologies. Includes a weekly laboratory practical taught by Ms. Carolyn Harrod and the biology department staff.
  • Essentials of Biology (BIOL 1303)

    3 semester hours, Fall semester

    An introduction to biology for non-science majors. The course covers evolution, early earth and the origins of life, prokaryotic diversity, eukaryotic diversity with a survey of the protists, plant life, fungi and animals. Includes a weekly laboratory taught by Ms. Carolyn Harrod and the biology department staff.
  • Evolution (BIOL 3303)

    3 semester hours, Spring semester

    An introduction to the principles of evolutionary analysis, a course intended for undergraduate biology and science majors. The course covers Darwinian evolution, natural, artificial and sexual selection, population genetics, and other classic themes in evolutionary biology.
  • Molecular Genetics Laboratory (BIOL 3222)

    2 semester hours, Spring semester

    A lecture-laboratory introduction to the principles of modern molecular genetic analysis intended for undergraduate biology majors. The objective of the course is to give students hands-on, practical experience in the modern experimental techniques used in biological, medical and forensic research. Students completing this course will have training in laboratory safety, recombinant DNA (gene cloning), genetic-DNA testing, biotechnological drug discovery and computer-based bioinformatics techniques.