B. Montgomery Pettitt


B. Montgomery Pettitt
Cullen Distinguished Professor of Chemistry
Professor of Physics, Computer Science, Biology and Biochemistry
Director of Institute of Molecular Design
Chair of Keck Center for Interdisciplinary Biology
Postdoctoral Fellow, Harvard University, 1983-1985
Postdoctoral Fellow, UT Austin, 1980-1983
Ph.D., University of Houston, 1980
B.S., University of Houston, 1975

Department of Chemistry
University of Houston
Houston, Texas 77204-5003

Office: 4027 - SERC
Phone: 713.743.3263

figure 1
(1) Development of methods for calculating internal conformational structure and interpreting conformational equilibria of biomolecules in aqueous environments.

(2) Stability and thermodynamics of DNA/RNA structures in solution and on surfaces both dielectric and metallic.

(3) Peptide/Protein folding via solution stability criteria. Theory of biomolecular solutions.

(4) Structural and thermodynamic description of molecular fluids, including water, ions, polar biomolecular solutes and other condensed phase systems via integral equation and density functional methods.

(5) Development of theoretical techniques for the description of the thermodynamics and structure of biomolecules as anisotropic fluids.

(6) Development of computer simulation methodology for material science and biotechnology.
figure 2 The solution environment as well as the sequence are known to determine the conformation, kinetic and thermodynamic behavior of polymers. It is widely appreciated for biopolymers that biological activity is usually found within a narrow range of solvent and salt concentration. Formulating hypotheses to explain this sensitivity is a unifying goal for the studies in the laboratory. The physical sensitivity is also reflected in a parameter sensitivity in theories and simulations of these systems which must be accounted for in any physical interpretations. Projects in this laboratory bring theoretical and calculational approaches to bear to an array of problems.


An area of considerable interest to us is how the presence of a surface, either, dielectric or metallic, affects the binding affinities between targets and probes. This is an improtant problem for optimizing DNA chips and Protein-chips. We have both theoretical and computational work which shows how one can optimize such surface effects to gain the most sensitivity in a DNA analysis.