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Orange Carotenoid Protein
Orange carotenoid protein (OCP) is a water-soluble protein which plays a role in photoprotection in diverse cyanobacteria. It is the only photoactive protein known to use a carotenoid as the photochemistry, photoresponsive chromophore. The protein consists of two domains, with a single carotenoid#Ketocarotenoids, keto-carotenoid molecule non-covalent interactions, non-covalently bound between the two domains. It is a very efficient Quenching (fluorescence), quencher of excitation energy absorbed by the primary light-harvesting complex, light-harvesting antenna complexes of cyanobacteria, the phycobilisomes. The quenching is induced by blue-green light. It is also capable of preventing oxidative damage by directly scavenging singlet oxygen (1O2). History OCP was first described in 1981 by Holt and David Krogmann, Krogmann who isolated it from the unicellular cyanobacterium ''Arthrospira maxima'', although its function would remain obscure until 2006. The crystal structure of t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photoprotection
Photoprotection is the biochemical process that helps organisms cope with molecular damage caused by sunlight. Plants and other oxygenic phototrophs have developed a suite of photoprotective mechanisms to prevent photoinhibition and oxidative stress caused by excess or fluctuating light conditions. Humans and other animals have also developed photoprotective mechanisms to avoid UV photodamage to the skin, prevent DNA damage, and minimize the downstream effects of oxidative stress. In photosynthetic organisms In organisms that perform oxygenic photosynthesis, excess light may lead to photoinhibition, or photoinactivation of the reaction centers, a process that does not necessarily involve chemical damage. When photosynthetic antenna pigments such as chlorophyll are excited by light absorption, unproductive reactions may occur by charge transfer to molecules with unpaired electrons. Because oxygenic phototrophs generate O2 as a byproduct from the photocatalyzed splitting ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photosystem
Photosystems are functional and structural units of protein complexes involved in photosynthesis. Together they carry out the primary photochemistry of photosynthesis: the absorption of light and the transfer of energy and electrons. Photosystems are found in the thylakoid membranes of plants, algae, and cyanobacteria. These membranes are located inside the chloroplasts of plants and algae, and in the cytoplasmic membrane of photosynthetic bacteria. There are two kinds of photosystems: PSI and PSII. PSII will absorb red light, and PSI will absorb far-red light. Although photosynthetic activity will be detected when the photosystems are exposed to either red or far-red light, the photosynthetic activity will be the greatest when plants are exposed to both wavelengths of light. Studies have actually demonstrated that the two wavelengths together have a synergistic effect on the photosynthetic activity, rather than an additive one.Each photosystem has two parts: a reaction center, w ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Orange Carotenoid N-terminal Domain
In molecular biology the orange carotenoid N-terminal domain is a protein domain found predominantly at the N-terminus of the Orange carotenoid protein (OCP), and is involved in non-covalent binding of a carotenoid chromophore. It is unique for being present in soluble proteins, whereas the vast majority of domains capable of binding carotenoids are intrinsic membrane proteins. Thus far, it has exclusively been found in cyanobacteria, among which it is widespread. The domain also exists on its own, in uncharacterized cyanobacterial proteins referred to as "Red Carotenoid Protein" (RCP). The domain adopts an alpha-helical structure consisting of two four-helix bundles. Orange carotenoid-binding proteins (OCP) were first identified in cyanobacterial species, where they occur associated with phycobilisome in the cellular thylakoid membrane. These proteins function in photoprotection, and are essential for non-photochemical quenching (NPQ). In full-length OCP, the NPQ activity is reg ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fluorescence Recovery Protein
Fluorescence recovery protein (FRP) is a small protein involved in regulating non-photochemical quenching in cyanobacteria. It prevents accumulation of the red photoactivated form of orange carotenoid protein (OCP), thereby reducing the amount of fluorescence quenching that occurs between the OCP and the phycobilisome antenna complexes. It interacts with the C-terminal domain of OCP, which shares homology with the NTF2 superfamily. Function FRP is constitutively active, both ''in vivo'' and ''in vitro''. It is able to prevent quenching of phycobilin fluorescence by OCP ''in vitro''. Overexpression of FRP in Synechocystis PCC 6803 leads to an absence of fluorescence quenching. Deletion mutants of FRP show a slightly larger degree of fluorescence quenching induced by strong blue-green light, but was unable to restore fluorescence levels when transferred to low-light or darkness. Structure The protein is all alpha-helical, and the protein structure from ''Synechocystis'' wa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Allophycocyanin
Allophycocyanin ("other algal blue protein"; from Greek language, Greek: '' (allos)'' meaning "other", '' (phykos)'' meaning “alga”, and '' (kyanos)'' meaning "blue") is a protein from the light-harvesting phycobiliprotein family, along with phycocyanin, phycoerythrin and phycoerythrocyanin. It is an accessory pigment to chlorophyll. All phycobiliproteins are water-soluble and therefore cannot exist within the membrane like carotenoids, but aggregate, forming clusters that adhere to the membrane called phycobilisomes. Allophycocyanin absorbs and emits red light (650 and 660 nm max, respectively), and is readily found in Cyanobacteria (also called blue-green algae), and red algae. Phycobilin pigments have fluorescent properties that are used in immunoassay kits. In flow cytometry, it is often abbreviated APC. To be effectively used in applications such as Fluorescence-activated cell sorting, FACS, High-Throughput Screening (HTS) and microscopy, APC needs to be chemically cro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metab ... 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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's Peptide, polypeptide chain that is self-stabilizing and that Protein folding, folds independently from the rest. Each domain forms a compact folded Protein tertiary structure, three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or Disulfide bond, disulfide bridges. Domains often form functional units, such as the calcium-binding EF-hand, EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimera (protein), chimeric ... [...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] |
Alpha Helix
An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the Protein secondary structure, secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right-handed helix conformation in which every backbone amino, N−H group hydrogen bonds to the backbone carbonyl, C=O group of the amino acid that is four residue (biochemistry), residues earlier in the protein sequence. Other names The alpha helix is also commonly called a: * Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure) * 3.613-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen) Discovery ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domains
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer after ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ribbon View Of The Orange Carotenoid Protein Structure 1M98
A ribbon or riband is a thin band of material, typically cloth but also plastic or sometimes metal, used primarily as decorative binding and tying. Cloth ribbons are made of natural materials such as silk, cotton, and jute and of synthetic materials, such as polyester, nylon, and polypropylene. Ribbon is used for useful, ornamental, and symbolic purposes. Cultures around the world use ribbon in their hair, around the body, and as ornament on non-human animals, buildings, and packaging. Some popular fabrics used to make ribbons are satin, organza, sheer, silk, velvet, and grosgrain. Etymology The word ribbon comes from Middle English ''ribban'' or ''riban'' from Old French ''ruban'', which is probably of Germanic origin. Cloth Along with that of fringes, and other smallwares, the manufacture of cloth ribbons forms a special department of the textile industry">textile industries. The essential feature of a ribbon loom is the simultaneous weaving in one loom frame of two or m ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Orange Carotenoid Protein Spectra Of Orange Vs Red Form
Orange most often refers to: *Orange (fruit), the fruit of the tree species '' Citrus'' × ''sinensis'' ** Orange blossom, its fragrant flower ** Orange juice *Orange (colour), the color of an orange fruit, occurs between red and yellow in the visible light spectrum *Some other citrus or citrus-like fruit, see ''list of plants known as orange'' * ''Orange'' (word), both a noun and an adjective in the English language Orange may also refer to: Arts, entertainment, and media Films * ''Game of Life'' (film), a 2007 film originally known as ''Oranges'' * ''Orange'' (2010 film), a Telugu-language film * ''The Oranges'' (film), a 2011 American romantic comedy starring Hugh Laurie * ''Orange'' (2012 film), a Malayalam-language film * ''Orange'' (2015 film), a Japanese film * ''Orange'' (2018 film), a Kannada-language film Music Groups and labels * Orange (band), an American punk rock band, who formed in 2002 from California * Orange Record Label, a Canadian independent record l ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
