Most drugs are comprised of small molecules that pass through cell membranes and are designed to bind to much larger protein molecules at exposed concave pockets. But in many disease-associated proteins, these binding sites are difficult to detect. Concave pockets may form only in the immediate presence of small molecules that bind to them (natural ligands or drugs) or are open only for brief periods during protein shape-shifting.
John Gross, PhD, Department of Pharmaceutical Chemistry, has been promoted to full professor.
Researchers in the Gross Lab combine a wide variety of molecular biology and quantitative biochemistry techniques with biophysics and structural biology experiments, such as NMR spectroscopy and X-ray crystallography, in order to understand how the composition, structure, and dynamics of multi-protein complexes affect their cellular function.
