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⚡ Robert huber nobel prize
„The most significant chemical reaction on Earth is photosynthesis.” In 1988, the Royal Swedish Academy of Sciences declared that Robert Huber, along with Hartmut Michel and Johann Deisenhofer, would be awarded the Nobel Prize in Chemistry. They decoded the three-dimensional structure of the photosynthetic reaction centre by working together. On February 20, Nobel Laureate and head of the Max Planck Institute (MPI) of Biochemistry’s emeritus working group “Structural Research” celebrated his 80th birthday. He has often been fascinated by the structure of proteins. His current study focuses on medications that can be used to treat autoimmune diseases.
Robert Huber, who was born on February 20, 1937, in Munich, grew up during the war: It was a tough time, with few schools and everyday struggles for bread and milk taking precedence. He learned to read and write on his own and with the aid of his family, and in 1947 he enrolled in one of the few grammar schools in the area of his parents’ home. Despite his parents’ financial struggles, he was able to study chemistry and complete his doctorate at the Technical University Munich thanks to scholarships (TUM).
👇 Robert huber max planck institute for biochemistry germany
Robert Huber (born February 20, 1937) is a Nobel Laureate in Biochemistry from Germany.
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      recognized for crystallizing an intramembrane protein essential in photosynthesis and then using X-ray
On February 20, 1937, he was born in Munich, where his father, Sebastian, worked as a bank cashier. From 1947 to 1956, he attended the Humanistisches Karls-Gymnasium and then went on to the Technische Hochschule to study chemistry, earning his diploma in 1960. He remained and worked on elucidating the structure of organic compounds using crystallography.
He shared the Nobel Prize in Chemistry with Johann Deisenhofer and Hartmut Michel in 1988. The trio was honored for their work in crystallizing an intramembrane protein involved in photosynthesis in purple bacteria and then using X-ray crystallography to determine its structure. [nine] The details offered the first glimpse into the structural bodies that were responsible for photosynthesis. This knowledge may be applied to the more complex analogue of photosynthesis found in cyanobacteria, which is nearly identical to that found in chloroplasts of higher plants. [requires citation]
Projects of Research Shift of electrons to semiconductor surfaces Optical Coherent Ranging (OCR) and Optical Coherence Tomography (OCT): imaging and profilometry using laser sources that sweep at a high frequency. Encoded in Time (TICO) Microscopy and Raman spectroscopy Spectral mode locking in optics and applications is known as Fourier Domain Mode Locking (FDML).
Postdoctoral research fellow of the German Research Foundation (DFG) in Prof. J. G. Fujimoto’s group at the Massachusetts Institute of Technology’s Research Laboratory of Electronics (M.I.T.)
🧔 Robert huber obituary
Professor Robert Huber’s research is primarily concerned with structural biology. He and two colleagues shared the Nobel Prize in Chemistry in 1988 for determining the three-dimensional structure of a photosynthetic reaction center in a bacterium. The methodological foundation of this study is x-ray crystallography, which allows researchers to resolve the three-dimensional structure of proteins down to the atomic level. Huber’s emeritus group “Structure Study” is also interested in biological structures, such as immune molecules, hormones, and enzymes.