Protein-bioconjugation reactions often suffer from poor specificity and poor reaction rates, especially when performed in the context of live cells or organisms. We are addressing these problems through genetic code expansion with amino acids that contain reactive handles that are not found in any of the common amino acids and that allow for fast and fully bioorthogonal conjugation reactions. For example, together with the Chin lab, we genetically encoded a norbornene lysine that enabled highly selective fluorescent labeling of a cell surface protein in human cells. We are currently expanding the toolset of bioconjugation reactions to other chemistries and the labeling with other probes.