Dr. Amzel’s research focuses on structural mechanistic biochemistry and structural thermodynamics. Amzel was the first to uncover the structure of part of an antibody, the molecule that helps the human immune system fight off infection. He was also part of a team of researchers at Johns Hopkins who produced the first high-resolution pictures of how antibodies interact with antigens, foreign molecules invading the body.

Since then, Amzel has determined the structure of many proteins and protein complexes. Amzel also studies how proteins fold and take on their three-dimensional shapes and how proteins catalyze biochemical reactions within cells. Some of his findings are being used to design drugs targeting the enzymes.

Dr. Amzel’s lab is studying the catalytic mechanism of several enzyme families, using molecular biology, biochemistry and structural biology. They are studying both enzymes that recognize or process phosphates and redox enzymes. Cloning and expression, ultrapurification, kinetic characterization, mutational analysis, mass spectrometry, crystallization, and structure determination by x-ray diffraction are some of the techniques the lab uses to characterize the mechanisms of these enzymes. As the team uncovers information about the enzyme systems, other researchers are designing new drugs based on their discoveries.

In addition to enzyme studies, Dr. Amzel’s lab studies structural thermodynamics. Researchers in his lab have developed several systems, including anti-peptide antibodies and lectins, to see how proteins interact and bond to macromolecules or ligands. They are developing computational methods to calculate the changes in the thermodynamic variables that take place when a protein recognizes another macromolecule or a small ligand. As research in this lab reveals more about binding energetics, other researchers can take that knowledge and apply it to structure-based drug design.