Prof. Sarel-Jacob Fleishman

Nature provides us with myriads of examples of exquisitely selective proteins that function as binders and enzymes. These proteins, however, are often formidably complex. For instance, a typical enzyme or the antigen-binding domain of an antibody comprise more than 200 amino acids and fold into complex three-dimensional conformations that depend critically on thousands of atomic interactions. By changing the protein sequence and structure or designing completely new proteins, we may generate desirable new enzymes for green chemistry, binders for research, diagnostics and therapeutics, and exquisite molecular sensors to measure metabolite concentrations. Visit our website.