Ongoing research projects are related to protein and RNA structure and dynamics, and RNA-protein interactions, with an emphasis on components of the protein synthesis apparatus. Nuclear magnetic resonance (NMR) spectroscopy is extensively used in our investigations.

Structural analysis of components of the translation initiation complex

The process by which the ribosome, tRNAs, initiation factors and elongation factors work together to synthesize a protein is of central importance within all forms of life. A detailed knowledge of the structure and interactions of these components will surely be required as part of a complete understanding of translation, and in particular, how the initiator tRNA and ribosome are brought together to initiate translation at the correct codon. Toward this goal, we have recently expressed and purified several of the most conserved components of the initiation complex, and analyses using multi-dimensional NMR and x-ray methods are underway.

Structural analysis of the RNase P complex

RNase P is a multi-component RNA-protein complex that cleaves the 5' termini of precursor tRNA in an essential step toward the synthesis of mature tRNA. The structure of RNase P is being determined using a combination of NMR and x-ray crystallographic methods, where the RNase P of Archaeoglobus fulgidus is being used as a model system.