Scott is currently a scientific software developer at Pfizer Inc.
Scott's postdoctoral research involved identifying the orientational landscape of antimicrobial peptides in biological membranes. This included identifying the roles of the peptide sequence and membrane composition in determining the peptide structure and orientation. This project was performed in close collaboration with experts in solid-state NMR spectroscopy, neutron scattering, and quartz crystal crystal microbalance measurements. His work contributed to identification of the surface-bound structure of the antimicrobial peptide piscidin, its curvature induction in four different lipid bilayers, and low aptitude for forming pores.
In Scott's graduate research, he demonstrated the role of the protein fold in redox proteins was to establish a low-dielectric cavity that buried the redox site away from the solvent and to establish a potential on the redox site specific to the polarization of the peptides in the protein backbone. The concepts developed in his graduate thesis have been incorporated into the Redox Module of CHARMMing, a web interface and teaching tool for the molecular mechanics program CHARMM.
Scott is deeply interested in the dissemination of basic scientific research and its practical application. He has participated in the NIH Entrepreneur and Commercialization Club, the NIH Games for Science Special Interest Group, and DC Tech Meetup. He has compiled a list of resources relating to biotech development in the Washington, DC area.