Protein recognition is
an important interaction in a variety of biological processes.
One type of protein interaction involves the hydrogen bonding of
one strand of a protein b -sheet to the exposed edge of another.
In Professor James Nowick’s research group, we develop small
molecules that assemble into dimers as way of mimicking b -sheet
interactions. This model has enabled us to control dimerization
affinity by designing mimics that vary in the number of hydrogen
bonds that they can form. To determine binding affinities, we utilize
nuclear magnetic resonance (NMR) techniques to measure the relative
proximity of each hydrogen atom. With this information, we can
understand dimer conformation, or binding mode, and calculate binding
constants for different b -sheet mimics. Continuing efforts in
this research may lead to a better understanding of protein interactions,
and ultimately a means of controlling these interactions.