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Heliorhodopsin
Heliorhodopsin is a family of rhodopsins discovered in 2018 by Alina Pushkarev in the laboratory of Professor Oded Beja. The new family of heliorhodopsins has a distinct protein sequence from known Type 1 (microbial) and Type 2 (animal) rhodopsins. Heliorhodopsins also exhibit the reverse orientation in the membrane compared with the other rhodopsins, with the N-terminus facing the inside of the cell and the C-terminus outside the cell. Heliorhodopsins use ''all-trans'' retinal as a chromophore, and do not have any ion pumping activity across the membrane. Heliorhodopsins are distributed globally and exist in eukaryotes, prokaryotes and even some viruses. Despite the wide distribution, Heliorhodopsins are never present in true diderms, where there is a proper double membrane around the microorganism. It has been suggested that the function of Heliorhodopsin requires a direct interaction with the environment. Crystal structures of Heliorhodopsins suggest they form a homodim ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heliorhodopsin
Heliorhodopsin is a family of rhodopsins discovered in 2018 by Alina Pushkarev in the laboratory of Professor Oded Beja. The new family of heliorhodopsins has a distinct protein sequence from known Type 1 (microbial) and Type 2 (animal) rhodopsins. Heliorhodopsins also exhibit the reverse orientation in the membrane compared with the other rhodopsins, with the N-terminus facing the inside of the cell and the C-terminus outside the cell. Heliorhodopsins use ''all-trans'' retinal as a chromophore, and do not have any ion pumping activity across the membrane. Heliorhodopsins are distributed globally and exist in eukaryotes, prokaryotes and even some viruses. Despite the wide distribution, Heliorhodopsins are never present in true diderms, where there is a proper double membrane around the microorganism. It has been suggested that the function of Heliorhodopsin requires a direct interaction with the environment. Crystal structures of Heliorhodopsins suggest they form a homodim ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heliorhodopsin Animation
Heliorhodopsin is a family of rhodopsins discovered in 2018 by Alina Pushkarev in the laboratory of Professor Oded Beja. The new family of heliorhodopsins has a distinct protein sequence from known Type 1 (microbial) and Type 2 (animal) rhodopsins. Heliorhodopsins also exhibit the reverse orientation in the membrane compared with the other rhodopsins, with the N-terminus facing the inside of the cell and the C-terminus outside the cell. Heliorhodopsins use ''all-trans'' retinal as a chromophore, and do not have any ion pumping activity across the membrane. Heliorhodopsins are distributed globally and exist in eukaryotes, prokaryotes and even some viruses. Despite the wide distribution, Heliorhodopsins are never present in true diderms, where there is a proper double membrane around the microorganism. It has been suggested that the function of Heliorhodopsin requires a direct interaction with the environment. Crystal structures of Heliorhodopsins suggest they form a homodim ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oded Beja
Oded Béjà is a professor in the Technion-Israel Institute of Technology, in the field of marine microbiology and metagenomics. Academic work Oded Béjà is best known for discovering the first bacterial rhodopsin naming it proteorhodopsin, during his postdoctoral fellowship in the laboratory of Edward DeLong. Oded Béjà's laboratory focuses currently on the role and diversity of photosynthetic viruses infecting cyanobacteria in the oceans, and the use of functional metagenomics for the discovery of new light sensing proteins. In 2018, the team of Oded Beja discovered a new family of rhodopsins with an inverted membrane topology, which can be found in bacteria, algae, algal viruses and archaea. Members of the new family were named heliorhodopsins. Early life and education Oded Béjà graduated with a B.Sc. degree from the Robert H. Smith Faculty of Agriculture, Food and Environment - Hebrew University of Jerusalem. He earned his M.Sc. and Ph.D. from the Weizmann Inst ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rhodopsin
Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene and a G-protein-coupled receptor (GPCR). It is the opsin of the rod cells in the retina and a light-sensitive receptor protein that triggers visual phototransduction in rods. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. When rhodopsin is exposed to light, it immediately photobleaches. In humans, it is regenerated fully in about 30 minutes, after which the rods are more sensitive. Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness. Names Rhodopsin was discovered by Franz Christian Boll in 1876. The name rhodospsin derives from Ancient Greek () for "rose", due to its pinkish color, and () for "sight". It was coined in 1878 by the German physiologist Wilhelm Friedrich Kühne (1837-1900). When George Wald discovered that rhodopsin is a holoprotein, consisting of retinal and an apoprotein, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Membrane
A membrane is a selective barrier; it allows some things to pass through but stops others. Such things may be molecules, ions, or other small particles. Membranes can be generally classified into synthetic membranes and biological membranes. Biological membranes include cell membranes (outer coverings of cells or organelles that allow passage of certain constituents); nuclear membranes, which cover a cell nucleus; and tissue membranes, such as mucosae and serosae. Synthetic membranes are made by humans for use in laboratories and industry (such as chemical plants). This concept of a membrane has been known since the eighteenth century but was used little outside of the laboratory until the end of World War II. Drinking water supplies in Europe had been compromised by the war and membrane filters were used to test for water safety. However, due to the lack of reliability, slow operation, reduced selectivity and elevated costs, membranes were not widely exploited. The first ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus. Chemistry Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an unbound amine group, the N-terminus. Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus. Function C-terminal retention signals While the N-terminus of a protein often ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinal
Retinal (also known as retinaldehyde) is a polyene chromophore. Retinal, bound to proteins called opsins, is the chemical basis of visual phototransduction, the light-detection stage of visual perception (vision). Some microorganisms use retinal to convert light into metabolic energy. In fact, a recent study suggests most living organisms on our planet ~3 billion years ago used retinal to convert sunlight into energy rather than chlorophyll. Since retinal absorbs mostly green light and transmits purple light, this gave rise to the Purple Earth Hypothesis. There are many forms of vitamin A — all of which are converted to retinal, which cannot be made without them. Retinal itself is considered to be a form of vitamin A when eaten by an animal. The number of different molecules that can be converted to retinal varies from species to species. Retinal was originally called retinene, and was renamed after it was discovered to be vitamin A aldehyde. Vertebrate animals ingest retin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chromophore
A chromophore is the part of a molecule responsible for its color. The color that is seen by our eyes is the one not absorbed by the reflecting object within a certain wavelength spectrum of visible light. The chromophore is a region in the molecule where the energy difference between two separate molecular orbitals falls within the range of the visible spectrum. Visible light that hits the chromophore can thus be absorbed by exciting an electron from its ground state into an excited state. In biological molecules that serve to capture or detect light energy, the chromophore is the moiety that causes a conformational change in the molecule when hit by light. Conjugated pi-bond system chromophores Just like how two adjacent p-orbitals in a molecule will form a pi-bond, three or more adjacent p-orbitals in a molecule can form a conjugated pi-system. In a conjugated pi-system, electrons are able to capture certain photons as the electrons resonate along a certain di ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Eukaryote
Eukaryotes () are organisms whose cells have a nucleus. All animals, plants, fungi, and many unicellular organisms, are Eukaryotes. They belong to the group of organisms Eukaryota or Eukarya, which is one of the three domains of life. Bacteria and Archaea (both prokaryotes) make up the other two domains. The eukaryotes are usually now regarded as having emerged in the Archaea or as a sister of the Asgard archaea. This implies that there are only two domains of life, Bacteria and Archaea, with eukaryotes incorporated among archaea. Eukaryotes represent a small minority of the number of organisms, but, due to their generally much larger size, their collective global biomass is estimated to be about equal to that of prokaryotes. Eukaryotes emerged approximately 2.3–1.8 billion years ago, during the Proterozoic eon, likely as flagellated phagotrophs. Their name comes from the Greek εὖ (''eu'', "well" or "good") and κάρυον (''karyon'', "nut" or "kernel"). E ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Prokaryote
A prokaryote () is a single-celled organism that lacks a nucleus and other membrane-bound organelles. The word ''prokaryote'' comes from the Greek πρό (, 'before') and κάρυον (, 'nut' or 'kernel').Campbell, N. "Biology:Concepts & Connections". Pearson Education. San Francisco: 2003. In the two-empire system arising from the work of Édouard Chatton, prokaryotes were classified within the empire Prokaryota. But in the three-domain system, based upon molecular analysis, prokaryotes are divided into two domains: ''Bacteria'' (formerly Eubacteria) and '' Archaea'' (formerly Archaebacteria). Organisms with nuclei are placed in a third domain, Eukaryota. In the study of the origins of life, prokaryotes are thought to have arisen before eukaryotes. Besides the absence of a nucleus, prokaryotes also lack mitochondria, or most of the other membrane-bound organelles that characterize the eukaryotic cell. It was once thought that prokaryotic cellular components within the c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Virus
A virus is a submicroscopic infectious agent that replicates only inside the living cells of an organism. Viruses infect all life forms, from animals and plants to microorganisms, including bacteria and archaea. Since Dmitri Ivanovsky's 1892 article describing a non-bacterial pathogen infecting tobacco plants and the discovery of the tobacco mosaic virus by Martinus Beijerinck in 1898,Dimmock p. 4 more than 9,000 virus species have been described in detail of the millions of types of viruses in the environment. Viruses are found in almost every ecosystem on Earth and are the most numerous type of biological entity. The study of viruses is known as virology, a subspeciality of microbiology. When infected, a host cell is often forced to rapidly produce thousands of copies of the original virus. When not inside an infected cell or in the process of infecting a cell, viruses exist in the form of independent particles, or ''virions'', consisting of (i) the genetic mate ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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