I am interested in structure-function studies on single-strand specific nucleic acid binding proteins (also known as helix-destabilizing proteins). As a class, the binding proteins have a wide range of biological roles, yet they share a number of biochemical commonalities. These include homologous functional domains, regions responsible for nucleic acid interaction, binding cooperativity, and interaction with other proteins.
The binding proteins under current investigation include bacteriophage T4 gene 32 protein, involved in DNA replication, recombination and repair, and the nucleocapsid (NC) proteins of retroviruses, which have a role in viral RNA packaging and replication, and act as “chaperones”, facilitators of nucleic acid conformational change. Gene 32 protein, historically one of the first of this class of proteins to be characterized, continues to provide us with fascinating insights.We are particularly concerned with the structural basis of binding cooperativity, the control of helix-destabilizing activity, and the interaction with other T4 replication, repair, and recombination proteins.
In our structure-function studies we employ a broad spectrum of experimental approaches, including biophysical, protein chemical, and molecular biological methodologies.