Robert Huber

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Robert Huber.

Robert Huber (born February 20, 1937 in Munich ) is a German chemist and Nobel Prize winner who made significant methodological contributions to the X-ray structure analysis of macromolecules , but above all clarified the atomic structure of a large number of interesting enzymes and structural proteins and thus made their functionality understandable Has.

Biography and work

Huber passed his Abitur in 1956 at the Humanist Karlsgymnasium in Munich-Pasing . He then studied chemistry at the Technical University of Munich (then TH) and received his doctorate there in 1963 under Walter Hoppe on the topic of X-ray structure analysis of syn-potassium methyldiazotate . Unlike many young colleagues in his field, he did not go to Max Perutz in Cambridge, who had received the Nobel Prize in 1962 for deciphering the structures of the oxygen transporter hemoglobin and was able to solve essential structural problems in X-ray structure analysis over the years, but instead worked at the Max Planck Institute for biochemistry in Martinsried near Munich set up an ambitious young team, but used Perutz's findings, developed them further and later became good friends with him.

He also wrote his habilitation with Hoppe in Munich. From 1971 to March 2005 he was director at the MPI in Martinsried. Today, as director emeritus, he heads the structural research group at the MPI for Biochemistry .

In 1988 he received the Nobel Prize for Chemistry together with Johann Deisenhofer and Hartmut Michel . All three were recognized for their first photosynthesis reaction center crystallization.

In his dissertation, Robert Huber deciphered the structure of ecdysone, a steroid hormone that controls the various moulting steps from the caterpillar to the finished insect. In Munich, he used the achievements of the Perutz team and expanded them so that they could be used to elucidate protein structures that consist not only of the previously usual ten to one hundred, but also thousands to ten thousand atoms.

The structure of the red oxygen-binding hemoprotein of the fly larva, which he deciphered with these methods in his habilitation thesis, showed, to everyone's surprise, a myoglobin-like chain fold, with which Huber proved for the first time the universality of the globin fold.

His entry into serine proteinases was in 1974 by determining the structure of the trypsin inhibitor from bovine pancreas (PTI). He and his team were able to determine the structure of this small, extremely stable protein with exceptional precision at the time, which is why it has long been an important reference structure for folding studies and simulation calculations.

The enzyme-inhibitor complexes turned out to be excellent examples of the interaction and mutual recognition of proteins, proteinases and smaller compounds, so that the first complete antibody of the IgG class could be elucidated in his department .

Huber and his team were able to use crystallographic means to show that proteins, which were viewed as rigid molecules in the 1970s, were in reality flexible and that was precisely what made many reactions possible in the first place. It is only the activation of the trypsinogen to trypsin that turns a partially disordered chain into an active, ordered protein conformation. Y- or T-shaped antibodies, on the other hand, offer examples of hinge movements of protein domains.

The opposite of this flexibility - rigidity - on the other hand, plays a decisive role in the function of two protein complexes that are involved in the first steps of the photosynthetic reaction: expansive light collector and light guide complexes capture light of different wavelengths and pass it on to the reaction centers through inductive resonance.

For the three-dimensional determination of this reaction center, he and his colleagues Johann Deisenhofer and Hartmut Michel received the Nobel Prize in Chemistry. They managed to decipher the structure of this intramembrane protein, which is important for photosynthesis in purple bacteria, with the help of X-ray structure analysis. Knowledge of these enables the first insight into the structural components that carry out the integral function of photosynthesis - and thus "one of the most fundamental processes in life". His understanding can be transferred to the even more complex, analogous processes during photosynthesis in cyanobacteria, which also take place in chloroplasts of higher plants.

The extraordinary productivity of this team in the elucidation of structures is in large part due to the further development of the methods of X-ray crystallography by Robert Huber. In addition to the "folding molecule method", the first area detector software MADNES and the crystallographic PROTEIN package, the department created the first functioning graphics system FRODO, which made it possible to superimpose and rotate three-dimensional electron clouds with structural models in order to access enzymes and Recognize substrates or antibodies and antigens complementary surface areas where enzymes dock to amino acids or other reactions can take place. Huber's success is based not least on his low fear of contact with new materials: he is not only an imaginative crystallographer, but also repeatedly carried out chemical experiments with dangerous materials and worked his way into the most diverse areas with which he had to do - up to and including for software development.

From 1976 to 2005 Huber was an adjunct professor at the Technical University of Munich, which appointed him Emeritus of Excellence in 2013. In addition, he holds several visiting professorships at the universities of Cardiff, Duisburg-Essen and Barcelona and is honorary professor at many (especially Southeast Asian) universities. He was a co-founder of the biotech companies Proteros (1997) and SuppreMol (2005), in both companies he has an advisory role. Robert Huber is a second marriage and has four children.

Awards and memberships (selection)


  • How I came to protease research or, more correctly, how protease research came to me , in: Angewandte Chemie Volume 125, Issue 1, pp. 69-75

Individual evidence

  1. biographical data, publications and Academic pedigree of Robert Huber at, accessed on February 12 2018th
  2. ^ Robert Huber: Structure of the Complex formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. II. Crystallographic refinement at 1.9 Å resolution . In: Journal of Molecular Biology . tape 89 , 1974, pp. 73-101 (English).
  3. Wolfram Bode, Robert Huber: Natural Protein Proteinase-Inhibitors and their Interaction with Proteinases . In: European Journal of Biochemistry . tape 204 , 1992, pp. 433-451 (English).
  4. ^ Robert Huber, Wolfram Bode: Structural Basis of Activation and Action of Trypsin . In: European Journal of Biochemistry . tape 11 , 1978, p. 114-122 (English).
  5. ^ Robert Huber - Facts. In: Nobel Media, July 9, 2020, accessed July 10, 2020 .
  6. ^ J. Deisenhofer, O. Epp, K. Miki, Robert Huber, H. Michel: Structure of the protein subunits in the photosynthetic reaction center of Rhodopseumdomonas viridis at 3Å resolution . In: Nature . tape 318 , 1985, pp. 618-624 .
  7. ^ Wolfram Bode, Hans Fritz: Robert Huber - A Life Devoted to Protein Structures and Functions . In: Biological Chemistry . tape 378 , 1997, pp. 119-120 .
  8. Press release. Nobel Media AB 2020. Thu. 9 Jul 2020.
  9. ^ Membership directory: Robert Huber. Academia Europaea, accessed June 29, 2017 (English, with biographical and other information).

Web links

Commons : Robert Huber  - Collection of images, videos and audio files