Protein structure and function, structural biology, magnetic resonance, metalloproteins.

More than 30% of all proteins in the cell exploit one or more metals to perform their specific functions, and over 40% of all enzymes contain metals. Metals are commonly found as natural constituents of proteins; however, many metal ions can be toxic when free in biological fluids. Hence, the human bodies as well as microorganisms have evolved considerable regulatory machinery to acquire, utilize, traffic, detoxify, and otherwise manage the intracellular and extracellular concentrations and types of metal ions. Despite the high regulation of metal ions in the human body, diseases such as Cancer, Menkes, Wilson, Alzheimer’s, Parkinson’s and Prion’s have been linked with metal binding to proteins.

Prof. Ruthstein’s lab utilizes various biophysical methods, such as EPR, NMR, CD, together with biochemical experiments, and computational methods to study the cellular copper cycle in detail in eukaryotic and prokaryotic systems. The knowledge gained is then used to develop novel biomarkers and therapeutic compounds. All experiments from the protein expression and purification stage till the cellular and mice level are conducted in house by the lab group members.

The main biophysical tool that is used in the lab of Prof. Ruthstein’s lab is pulsed EPR spectroscopy. The power of EPR lies in the sensitivity to both atomic level changes and nanoscale fluctuations. EPR can characterize properties such as redox state and ligand geometry for different functional states of the protein. In addition, EPR can measure distances between paramagnetic probes up to 80 Å