Jeremy M. Berg
Board Member: 2014-2016
Macromolecular structure and function; metalloproteins; nucleic acid binding proteins
We are interested in understanding the various roles that metal ions play in biological systems. Of particular current interest are several large families of proteins that contain structural domains stabilized by bound zinc ions. Included among these proteins are molecules of obvious biomedical interest, including the products of several oncogenes, the steroid hormone receptors and proteins involved in RNA packaging in retroviruses.
The projects currently underway in the laboratory include structural studies of several of these metal binding domains using two-dimensional nuclear magnetic resonance methods, metal binding studies directed towards understanding which metals ions can be bound by these proteins and how the binding preferences are determined, nucleic acid binding studies aimed at determining how proteins that contains these domains accomplish sequence specific nucleic acid binding, sequence variation studies designed to determine what sequence features dictate the metal binding and structural properties of these domains and molecular biological studies of the occurrence and functions of proteins that contain these domains in a variety of organisms. The combination of this wide range of approaches is providing insights into how these proteins function in biological systems and into more general issues of proteins folding and molecular recognition.