Research Priorities: Protein structures, photosynthetic reaction centre, photosynthesis, crystal structures, X-ray crystallography, immune molecules, proteases, drug design programmes

Robert Huber is a German chemist, working primarily on research into protein structures. In 1988 he received, jointly with the German biophysicist Johann Deisenhofer and the German biochemist Hartmut Michel, the Nobel Prize in Chemistry for decoding the three-dimensional structure of the photosynthetic reaction centre of purple bacteria. With their work, the researchers have provided fundamental insights into photosynthesis.

Robert Huber and his colleagues were able to crystallise the reaction centre of the bacterium Rhodopseudomonas viridis (Blastochloris viridis). It was the first ever membrane protein complex of which the atomic structure could be analysed by X-ray crystallography. From the results of this research it has been possible to explain how plant cells store energy from the sun. It was also possible to apply the result to plants, as the photosynthetic reaction centre of the bacterium has almost the same structure as higher plants.

In the 1970s Robert Huber set up the first protein crystallography laboratory in Germany and, using X-ray crystallography, has been able to reveal more than 100 protein structures over the years, including proteins of the immune system and of energy and electron transfer. A further priority of his scientific research has been the development of new analytical instruments and methods. As Emeritus of the Group “Structure Research” at the Max Planck Institute of Biochemistry, he mainly studies proteases and immune molecules and works in the field of drug research on “drug design” programmes for the development of new active substances.