Ned Budisa applies the Selective Pressure Incorporation method that enables single and multiple in vivo incorporations of synthetic amino acid analogs in proteins, preferably by sense codon reassignment. His methodology allows for fine chemical manipulations of the amino acid side chains, mainly of proline, tryptophan and methionine. These experiments are often assisted with simple metabolic engineering. Ned's research goal is the transfer of various physicochemical properties and bioorthogonal chemistry reactions as well as special spectroscopic features into the proteins of living cells. In addition, his method allows the delivery of element-specific properties into the biochemistry of life. Ned Budisa is well known for the establishment of the use of selenium-containing non-canonical amino acids for protein X-ray crystallography and fluorine-containing analogs for 19F NMR-spectroscopy and protein folding studies. He was the first to demonstrate the use of genetic code engineering as a tool for the creation of therapeutic proteins and ribosomally synthetized peptide-drugs. He has succeeded with innovative engineering of biomaterials, in particular photoactivatable mussel-based underwater adhesives. Ned Budisa made seminal contributions to our understanding of the role of methionine oxidation in prion protein aggregation and has discovered the roles of proline side chain conformations in translation, folding and stability of proteins. Together with his co-worker Vladimir Kubyshkin, the new-to-nature hydrophobic polyproline-II helixfoldamer was designed. Along with Budisa's previous work on bioexpression using proline analogues, the results of this project contributed to the establishment of the Alanine World hypothesis. It explains why nature chose the genetic code with "only" 20 canonicalamino acids for ribosomal protein synthesis. In 2015, the team led by Ned Budisa reported the successful completion of a long-term evolution experiment that resulted in full, proteome-wide substitution of all 20,899 tryptophan residues with thienopyrrole-alanine in the genetic code of the bacterium Escherichia coli. This is a solid basis for the evolution of life with alternative building blocks, foldamers or biochemistries. At the same time, this approach might be an interesting biosafety technology to evolve biocontained synthetic cells equipped with a "genetic firewall" which prevents their survival outside of man-made unnatural environments. Similar experiments with flourinated tryptophan analogs as xenobiotic compounds has led to the discovery of exceptional physiological plasticity in microbial cultures during adaptive laboratory evolution, making them potential environmentally friendly tools for new bioremediation strategies. Ned Budisa is also actively involved in the debate of possible societal, ethical and philosophical impacts of radical genetic code engineering in the context of synthetic cells and life as well as technologies derived thereof.