Robert Huber
Robert Huber Technical University Munich | |
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Known for | Cyanobacteria Crystallography |
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Scientific career | |
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Website | www |
Robert Huber (German pronunciation:
Education and early life
He was born on 20 February 1937 in
Career
In 1971 he became a director at the
In 1988 he received the
In 2006, he took up a post at the Cardiff University to spearhead the development of Structural Biology at the university on a part-time basis.[13]
Since 2005 he has been doing research at the Center for medical biotechnology of the University of Duisburg-Essen.
Huber was one of the original editors of the Encyclopedia of Analytical Chemistry.
Awards and honours
In 1977 Huber was awarded the
Huber has built up, led and still leads the most productive protein crystallography laboratory in Europe. His own contributions to crystallography, made over a period of some 25 years, are prodigious. For his PhD thesis he solved the chemical formula of the important insect hormone edtyson which had eluded the chemists. He then demonstrated that the tertiary fold of the polypeptide chain in the haemoglobin of the fly larva chironomus closely resembled that in Kendrew's sperm whale myoglobin
Huber's next achievement was the solution of the structure of trypsin inhibitor and the demonstration that in its complex with trypsin it mimicked the tetrahedral transition state of the enzyme's substrate. Since then he has determined the structures of many other proteinases, their inactive precursors and their inhibitors, and has established himself as the world authority in this field. Outstanding structures are those of procarboxypeptidase, which led to the discovery of the remarkable activation mechanism of this enzyme, and of the complex of thrombin with hirudin, which showed the molecular mechanism of inhibition of blood clotting by this leech toxin.
In parallel with this work, Huber solved the structures of several
Huber's structure of citrate synthase revealed a striking example of a conformational change undergone by an enzyme on combination with its substrate by a process of induced fit. Huber shared the Nobel Prize for Chemistry in 1988 with Michel and Deisenhofer for their determination of the remarkable and supremely important structures of the photochemical reaction centre of Rhodopseudomonas viridis and of phycocyanin, the light harvesting protein of the blue-green alga Mastiglocadus laminosus. This protein binds linear tetrapyrroles in a tertiary fold reminiscent of the globins, which brought Huber back full circle to his first structure, erythrocruerin, Huber has also determined the structures of several copper-containing electron-transfer proteins, including that of ascorbate oxidase, and of other metallo-enzymes. These studies have thrown new light on electron-transfer systems and on zinc coordination in proteins. He has also solved the structure of an important class of calcium binding proteins – the annexins. Finally his very accurate structures have provided important insights into the different degrees of mobility within protein molecules.
Huber has published some 400 papers.[1]
Personal life
Huber is married and has four children.[citation needed]
References
- ^ a b "Certificate of election EC/1999/43: Huber, Robert". London: Royal Society. Archived from the original on 2019-07-08.
- ^ a b "Professor Robert Huber ForMemRS". London: Royal Society. Archived from the original on 2015-10-26.
- S2CID 4193312.
- PMID 964922.
- PMID 1255713.
- .
- S2CID 4261663.
- PMID 6392571.
- ^ Robert Huber autobiographical information at www.nobel.org
- PMID 9537320.
- S2CID 1551692.
- S2CID 23034289.
- ^ Smith, Alexandra (2006-10-24). "Nobel chemist joins Cardiff University". The Guardian. Retrieved 14 September 2015.
- ^ "Otto-Warburg-Medal". GBM. Retrieved 12 January 2014.
- ^ "Superstars of Science". Retrieved 12 January 2015.
- ^ "Curriculum vitae". Max Planck Institute. Retrieved 11 January 2015.
External links
- Robert Huber on Nobelprize.org