A variety of opportunities are available for experimental, computational, and theoretical research in the following areas: (1) structural determinations of small (2-10 kD) or large protein toxins by biomolecular nuclear magnetic resonance (NMR) spectroscopy and molecular modeling, (2) structural determinations of large protein toxins (>20 kD) and ligand-toxin complexes by x-ray crystallography, (3) protein toxin conformational dynamics investigated by biomolecular NMR spectroscopy and molecular dynamics simulations, (4) evaluation of the conformational changes and associated thermodynamics on ligand-toxin and macromolecule-toxin binding by NMR spectroscopy and molecular dynamics simulations, and (5) rational design of toxin binding ligands and nanoparticles by computational and computer modeling methods. Additional related interests include protein folding and the evolution of protein conformational flexibility. Research is conducted at Edgewood and at several collaborator sites, including the Army Research Laboratory High-Performance Computing Center (Aberdeen Proving Ground, MD), the New York Structural Biology Center (New York, NY), and the University of Central Florida Nanoscience Technology Center (Orlando, FL). This research focuses on developing a new generation of robust toxin sensors and target-specific decontamination systems for military and homeland security applications.

 

key words

Biophysics; Biosensor design; Computational chemistry; Conformational dynamics; Molecular modeling; Nanoparticle design; Nuclear magnetic resonance spectroscopy; Protein structure; X-ray crystallography;

Citizenship:  Open to U.S. citizens

Level:  Open to Postdoctoral and Senior applicants