Robert Huber

HPLC. See High performance liquid chromatography HSQC 144 Huber, Robert 84 Human body, elements in 31 Human genome 12, 201 Human glucose transporters 416 figure 416... 

HUBER, ROBERT (1937-). Awarded the Nobel prize lor chemistry in 1988. along with Johann Deisenhofer and Hartmut Michel, for work that revealed the chree-dimensional structure of closely linked proteins that are essential to photosynthesis. Doctorate awarded in 1963 by Technical University of Munich. Germany. 

Huber, Robert (b. 1937) German biochemist who helped to determine antibody structure and binding sites showed that there was a very small structural difference between the active and the inactive form of the enzyme phosphorylase and, with Hartmut Michel and Johann Deisenhofer, worked out the detailed structure of the membrane-bound region where photosynthesis occurs in the purple bacterium Rhodopseudomonal viridans. For this work, he and his colleagues were awarded the 1988 Nobel Prize in chemistry. 

See, e.g., Robert W. Crandall, Controlling Industrial Pollution (1983) Peter W. Huber Robert E. Litan, The Liability Maze (1991) Lester B. Lave, The Strategy of Social Regulation (1981). 

Figure 2.14 shows examples of both cases, an isolated ribbon and a p sheet. The isolated ribbon is illustrated by the structure of bovine trypsin inhibitor (Figure 2.14a), a small, very stable polypeptide of 58 amino acids that inhibits the activity of the digestive protease trypsin. The structure has been determined to 1.0 A resolution in the laboratory of Robert Huber in Munich, Germany, and the folding pathway of this protein is discussed in Chapter 6. Hairpin motifs as parts of a p sheet are exemplified by the structure of a snake venom, erabutoxin (Figure 2.14b), which binds to and inhibits... 

What molecular architecture couples the absorption of light energy to rapid electron-transfer events, in turn coupling these e transfers to proton translocations so that ATP synthesis is possible Part of the answer to this question lies in the membrane-associated nature of the photosystems. Membrane proteins have been difficult to study due to their insolubility in the usual aqueous solvents employed in protein biochemistry. A major breakthrough occurred in 1984 when Johann Deisenhofer, Hartmut Michel, and Robert Huber reported the first X-ray crystallographic analysis of a membrane protein. To the great benefit of photosynthesis research, this protein was the reaction center from the photosynthetic purple bacterium Rhodopseudomonas viridis. This research earned these three scientists the 1984 Nobel Prize in chemistry. 

Matthias Bochtler, Michael Croll, Hans Brandstetter, Tim Clausen, and Robert Huber... 

Huber, Peter. 1988a. Environmental Hazards and Liability Law. In Liability Perspectives and Policy. Edited by Robert E. litan and Clifford Winston. Washington Brookings Institution. 

Johan Diesenhofer, Robert Huber, and Hartmut Michel Chemistry Three-dimensional structure of a photosynthetic reaction center... 

A) Top view of the 20S protea-some as an a-carbon plot showing the seven-fold symmetry. The a subunits are in front of the 3 subunits. (B) Side view showing the proteasome cut open along its seven-fold axis. From Lowe et al.dd Courtesy of Robert Huber. 

Figure 13-8 Three-dimensional structure of citrate synthase. (A) Stereoscopic alpha carbon trace of the dimeric pig enzyme in its open conformation.209 A molecule of citrate is shown in the lower subunit. The view is down the two-fold axis. Courtesy of Robert Huber.

For many years, die nature and location of the complex of proteins (sometimes referred to as the engine of photosynthesis) were poorly understood. During the 1980s, much more was learned as the result of research carried out by Johann Deisenhofer (Howard Hughes Medical Institute), Robert Huber, and Harmut Michel (Max Planck Institute), and for this work the investigators were awarded the 1988 Nobel Prize for chemistry. The protein complex, called the membrane-bound proteins, are difficult to define structurally because they do not crystallize readily and thus could not be subjected to x-ray crystallography. However, over a period of three years, the researchers were able to create crystals and thus were able to determine precisely the position of some 10,000 atoms in the protein complex. 

The crystal structure of reaction centers from R. viridis was determined by Hartmut Michel, Johann Deisenhofer, Robert Huber, and their colleagues in 1984. This was the first high-resolution crystal structure to be obtained for an integral membrane protein. Reaction centers from another species, Rhodobacter sphaeroides, subsequently proved to have a similar structure. In both species, the bacteriochlorophyll and bacteriopheophytin, the iron atom and the quinones are all on two of the polypeptides, which are folded into a series of a helices that pass back and forth across the cell membrane (fig. 15.1 la). The third polypeptide resides largely on the cytoplasmic side of the membrane, but it also has one transmembrane a helix. The cytochrome subunit of the reaction center in R. viridis sits on the external (periplasmic) surface of the membrane. 

The vinyl silanized samples from Mr. Robert E. Schultz of J. M. Huber had been prepared as follows liquid vinylmethoxyethoxy silane (Union Carbide A172) was quantitatively added to a known volume of a mixture of 60% de-ionized water and 40% 2-propanol in a polyethylene beaker via a disposable polyethylene syringe. 100 g of ATH (aluminum trihydrate) was stirred into exactly 300 ml of the vinyl silane mixture for 10 min with a polyethylene rod. The resulting slurry was placed in a 100°C oven and allowed to dry for 24 h. 

The authors are greatly indebted to Mr. Robert E. Schultz, from the J. M. Huber, Solem Division, Fairmount, GA, who supplied the eight vinyl silanized aluminum hydroxide powder samples used in this study, and details of their preparation. 

Animals consume chlorophyll lied Nazis) Hans Robert Huber Hartmut... 

The Nobel Prize in chemistry was awarded to Johan Deisenhofer, Robert Huber, and Hartmut Michel in 1988 for unraveling the structure of the reaction center from the purple photosynthetic bacterium Rhodopseudomonas viridis using X-ray crystallography. 

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