Research

Members of the Donald Lab are conducting research in:

Computational Biology & Chemistry »

Some of the most challenging and influential opportunities for Physical Geometric Algorithms (PGA) arise in developing and applying information technology to understand the molecular machinery of the cell. Our recent work shows that many PGA techniques may be fruitfully applied to the challenges of computational molecular biology. PGA research may lead to computer systems and algorithms that are useful in structural molecular biology, proteomics, and rational drug design. Concomitantly, a wealth of interesting computational problems arise in proposed methods for discovering new pharmaceuticals. [More]

We also have some interest in other areas, including:

Microelectromechanical Systems (MEMS) and Microrobotics »

The goal of this research is to build microsystems that can actively, accurately, and efficiently interact and change the physical world. While so far MEMS research has been biased more towards sensor technology, there are a large number of potential applications that require micro actuators. Important examples are techniques to efficiently move, sort, or mix small particles (e.g. cells in applications); or micro positioning devices for inspection and assembly of complex micro systems (e.g. for display or amplifier arrays). [More]

Other Research »

See Our Papers and Books for a full list of the research topics we have been interested in.

Protein Design

Redesigning the PheA Domain of Gramicidin Synthetase. Biochemistry 2006; 45(51).

Protein Structures

Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis. PDB ID: 1QZF (J. Biol. Chem.)

Complete ensemble of NMR structures of the unphosphorylated human cardiac phospholamban pentamer. PDB ID: 2HYN (Proteins, 2006)

Microelectromechanical Systems

Untethered, Electrostatic, Globally-Controllable MEMS Micro-Robot. Journal of Microelectromechanical Systems 2006; 15(1)

Allosteric Inhibition of the Protein-Protein Interaction Between the Leukemia-Associated Proteins RUNX1 and CBFß. Chemistry & Biology (2007).