Gerhard Wagner

Performed the first comprehensive study of hydrogen exchange on a protein using NMR and showed internal amides exchange via unfolding. Developed strategies that enabled the assignment of the NMR spectra of proteins and mapped their internal motions critical for protein function. Discovered aromatic rings flip rapidly in otherwise rigid proteins. Played the key role in development of the technology for protein structure determination in solution and made major contributions to triple resonance NMR spectroscopy, based on isotopic enrichment of cloned proteins, universally used for protein NMR studies. Determined more than 60 NMR protein structures, including essential proteins for human translation initiation, components of the T-cell receptor complex and the voltage dependent anion channel of the outer mitochondrial membrane. Discovered small-molecule inhibitors of translation initiation that have anti-tumor activity.