Research in Dr. Rainey’s lab focuses on developing molecular- and atomic-level understanding of biological processes involving proteins. A variety of structural biology techniques are exploited, including NMR spectroscopy and scanning probe microscopy alongside computation in order to use biophysical results. Dr. Rainey tackles two classes of protein that function in supramolecular assemblies: membrane proteins and fibrous proteins. In the realm of membrane proteins, he currently focuses on: (1) the apelin receptor (APJ), a G-protein coupled receptor, its peptidic ligands and the processing of precursors of these ligands to produce bioactive forms; and, (2) the fusion-associated small transmembrane (FAST) proteins, a recently identified family of uniquely small viral membrane fusion proteins. Dr. Rainey’s main fibrous protein of focus at the moment is a recombinant protein based on the type of silk spiders use to wrap their prey. This also happens to be one of the toughest known materials. He also uses peptide synthesis and recombinant protein expression to engineer peptides capable of self-assembly that are inspired by collagen and intermediate-filament proteins. Apart from all this, Dr. Rainey’s lab has fun developing NMR methods to characterize other materials, such as soft polymeric nanoparticles.