EAGER: Backbone Selenoamides as Minimal Chromophores to Monitor Protein Dynamics

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In this project funded by the Chemistry of Life Processes Program of the Chemistry Division, James Petersson of the University of Pennsylvania will study the molecular details of rapid protein motions that underlie cellular communication. To track these motions, the Petersson laboratory is developing novel, "non-invasive" probes that will allow them to monitor changes in protein structure with increased levels of temporal and structural resolution, with the long-term goal of creating atomic-scale movies of protein motions. These probes consist of single-atom substitutions (sulfur or selenium) to the amide bond that links every amino acid in a protein. The novelty of the probes lies in their small size, so that unlike many current probes, they will not perturb the motion they are meant to study. The broader impacts involve training undergraduate and graduate students in a multidisciplinary laboratory environment that makes use of organic synthesis, physical chemistry, molecular, and cellular biology to investigate biological phenomena. Our goals also include broadening participation through increased inclusion of women researchers, and continuing to build the summer REU program for underrepresented minorities at the University of Pennsylvania Laboratory for Research on the Structure of Matter (LRSM). The molecular rearrangements to be studied are not only important to cell signaling, but are fundamental to all complex macromolecules, biological or synthetic. Thus, these tools can be of utility to the biochemical community wishing to study protein motion and may improve our ability to design molecular motors from first principles.