Jonah Cheung is a senior scientist at the New York Structural Biology Center (NYSBC). He earned his Ph.D. in 2005 and continued postdoctoral studies at Columbia University in the Department of Biochemistry and Molecular Biophysics, where he focused on the study of bacterial transmembrane histidine kinase sensor proteins using a structural genomics approach.

Cheung has a broad background in biochemistry and biophysics, with extensive training and expertise in X-ray crystallography of macromolecules and is proficient in all stages of the structure solution pipeline. He joined NYSBC in 2010 and now leads the Special Projects Group, which focuses on structure determination and biophysical and biochemical characterization of protein targets from numerous biological systems, including enzymes and enzyme complexes, soluble domains of membrane proteins and receptors, and antibody-antigen complexes.

Cheung developed a method of crystallization of human acetylcholinesterase, allowing for rapid structure determination of pharmacologically relevant complexes with small molecule ligands. As structural studies of acetylcholinesterase were traditionally limited to nonhuman homologs, this groundbreaking work laid a foundation for structure-based design of medical countermeasures against chemical warfare nerve agents that specifically target the human enzyme.

Cheung also applied his expertise to the structural study of two recurring mutants of cAMP-dependent protein kinase A, which had been found through exome sequencing to be associated with tumors in livers and kidneys. His work provided atomic-level understanding and revealed two distinct, underlying disease mechanisms in these two types of tumors, which were previously thought to be caused by similar molecular dysfunctions.