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Bacteriorhodopsin is a protein used by Archaea, ..

They are predominantly synthesized in nature by photosynthetic organisms and some non-photosynthetic eubacteria.

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It is the retinal molecule that changes its conformation when ..

Thus a human gene can be expressed in bacteria or yeast or jelly fish, and jelly fish genes can be expressed in bacteria, plants, fungi, animals and protists.

Some immune cells use lysosomes to destroy viruses and bacteria that they take in through .

Therefore bacterio- and proteorhodopsin-mediated phototrophicgrowth results in “proton transport phosphorylation, incontrast to the “electron transportphosphorylation” of the classical photosynthesis.

Phototrophy | Boundless Microbiology

These bacteria are important for proper digestion and fecal excretion of waste products.

When Hartmut Michel's group began work on crystallizing LH2, another researcher at the University of Glasgow began similar determination of the structure of LH2 as well, but for a different bacterium. The British scientist, Richard Cogdell, worked on structure determination for the species Rhodopseudomonas acidophila. On the other hand, Hartmut Michel had chosen to work on LH2 of the bacterium Rhodospirillum molischianum, a decision that would have profound consequences.

In the same year that he jump-started his return to photosynthesis by publishing computational papers that utilized the new reaction center structure, Schulten took a job at the University of Illinois at Urbana-Champaign. Soon after that, in 1989, Schulten founded the Theoretical Biophysics Group there at the Beckman Institute for Advanced Science and Technology, an interdisciplinary center at the university. Eventually the group at Beckman became known as the Theoretical and Computational Biophysics Group. It is through this group that Schulten and collaborators were able to start to piece together the many steps in photosynthesis and begin to understand it on a grand scale

The Importance of Photosynthesis

To conquer the problem, Hu and Schulten first generated a structure that they hoped was similar to the real structure, which they called a “search model,” and which they based on the Rps. acidophila structure that had already been determined by Cogdell's group. The experimentalists in Michel's group were experts in reading diffraction data, and surmised that the structure of the light-harvesting complex was a ring made of eight identical subunits, which effectively reduced the problem to one-eighth of its original complexity. So Hu and Schulten only needed to solve the structure for one subunit in the protein, and they could utilize Cogdell's structure as a guide. In essence Hu and Schulten used a computational step to generate search models that were homologous to the unknown structure so they could determine the phases. Schulten likens the procedure to iterating with Newton's Method: if the answer diverges, one can clearly see the initial guess was far off and so one starts over with a different guess. Hu says that what finally solved the structure was exploiting the symmetry aspects of the protein. The structure they computed is shown at left.

But Hartmut Michel was not discouraged by his setbacks with bacteriorhodopsin. He decided to find more suitable membrane proteins and try and crystallize them instead. He chose to work with reaction center proteins from two purple bacteria, and also chlorophylls from spinach. He knew that these protein complexes were said to be part of crystalline arrays in their native environment. Using detergents, and techniques acquired from the bacteriorhodopsin work, in July 1981 Michel finally formed three-dimensional crystals of the reaction center protein of purple bacteria Rhodopseudomonas viridis. But the big test would be whether or not the reaction center crystals were of suitable quality for X-ray diffraction. In September of that year, working with Wolfram Bode, Michel found his crystals diffracted beautifully. Three years after Michel had accidentally observed crystalline-like membrane proteins in a freezer, he finally succeeded in producing high-quality crystals of a membrane protein, a task purported to be impossible. Michel points to 1981 as one of the best years of his life.

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  • PHOTOSYNTHESIS - Estrella Mountain Community …

    How are purple and green phototrophic bacteria able to use such a widevariety of light wavelengths for photosynthesis?

  • PHOTOSYNTHESIS Table of Contents ..

    Bacteria and Archaea

  • Prokaryotic photosynthesis and phototrophy …

    it’s not a bacteria), that uses a different chemical for its photosynthesis and that chemical is retinal.

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Prokaryotic photosynthesis and phototrophy ..

In contrast to thephotosynthesis of endosymbiontic chloroplasts in plants and previouslyknown groups of photosynthetic bacteria no electron transport isinvolved.

Anoxygenic photosynthesis photosynthesis ..

Bacteria are also known as prokaryotes (together with archaea; formerly archaebacteria) referring to the single compartment inside the cell and missing a membrane delineated cell nucleus found in all eukaryotes.

19/12/2017 · Comparison of Retinal ..

Cells are surrounded by a cell membrane (and cell wall in bacteria and plants = a membrane plus some chemically more stable structures, often mixtures of proteins and polysaccharides) and contain all necessary elements to sustain life; proteins, nucleic acids, lipids, minerals, and a diverse class of metabolites.

1993), whereas in purple bacteria ..

Outline the steps in methanogesis from CO2

Describe at least 5 differences between anoxygenic (purple and green)and oxygenic (cyanobacteria) phototrophic bacteria.

From photosynthesis to new compounds for eye …

Cloning is a natural process that underlies asexual reproduction that include the binary fission of prokaryotic cells (bacteria and archaea) and mitotic cell division of eukaryotic cells.

Photo System | Photosynthesis | Chloroplast

β-carotene can be seen close to the reaction center of Photosystem II (left), and (an acyclic carotenoid with a sugar attached), associated with the Light Harvesting Chlorophyll Protein 2 (LH II) of , a photosynthetic purple bacteria (right).

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