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Allophycocyanin
Allophycocyanin ("other algal blue protein"; from 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 & 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 FACS, High-Throughput Screening (HTS) and microscopy, APC needs to be chemically cross-linked. Structural characteristics Allophycocyani ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phycocyanin
Phycocyanin is a pigment-protein complex from the light-harvesting phycobiliprotein family, along with allophycocyanin and phycoerythrin. It is an accessory pigment to chlorophyll. All phycobiliproteins are water-soluble, so they cannot exist within the membrane like carotenoids can. Instead, phycobiliproteins aggregate to form clusters that adhere to the membrane called phycobilisomes. Phycocyanin is a characteristic light blue color, absorbing orange and red light, particularly near 620 nm (depending on which specific type it is), and emits fluorescence at about 650 nm (also depending on which type it is). Allophycocyanin absorbs and emits at longer wavelengths than phycocyanin C or phycocyanin R. Phycocyanins are found in cyanobacteria (also called blue-green algae). Phycobiliproteins have fluorescent properties that are used in immunoassay kits. Phycocyanin is from the Greek '' phyco'' meaning “algae” and ''cyanin'' is from the English word “cyan", which conven ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Time-resolved Fluorescence Energy Transfer
Time-resolved fluorescence energy transfer (TR-FRET) is the practical combination of time-resolved fluorometry (TRF) with Förster resonance energy transfer (FRET) that offers a powerful tool for drug discovery researchers. TR-FRET combines the low background aspect of TRF with the homogeneous assay format of FRET. The resulting assay provides an increase in flexibility, reliability and sensitivity in addition to higher throughput and fewer false positive/false negative results. FRET involves two fluorophores, a donor and an acceptor. Excitation of the donor by an energy source (e.g. flash lamp or laser) produces an energy transfer to the acceptor if the two are within a given proximity to each other. The acceptor in turn emits light at its characteristic wavelength. The FRET aspect of the technology is driven by several factors, including spectral overlap and the proximity of the fluorophores involved, wherein energy transfer occurs only when the distance between the donor an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phycobiliprotein
Phycobiliproteins are water-soluble proteins present in cyanobacteria and certain algae (rhodophytes, cryptomonads, glaucocystophytes). They capture light energy, which is then passed on to chlorophylls during photosynthesis. Phycobiliproteins are formed of a complex between proteins and covalently bound phycobilins that act as chromophores (the light-capturing part). They are most important constituents of the phycobilisomes. Major phycobiliproteins Characteristics Phycobiliproteins demonstrate superior fluorescent properties compared to small organic fluorophores, especially when high sensitivity or multicolor detection required : * Broad and high absorption of light suits many light sources * Very intense emission of light: 10-20 times brighter than small organic fluorophores * Relative large Stokes shift gives low background, and allows multicolor detections. * Excitation and emission spectra do not overlap compared to conventional organic dyes. * Can be used in tandem ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phycoerythrin
Phycoerythrin (PE) is a red protein-pigment complex from the light-harvesting phycobiliprotein family, present in cyanobacteria, red algae and cryptophytes, accessory to the main chlorophyll pigments responsible for photosynthesis.The red pigment is due to the prosthetic group, phycoerythrobilin, which gives phycoerythrin its red color. Like all phycobiliproteins, it is composed of a protein part covalently binding chromophores called phycobilins. In the phycoerythrin family, the most known phycobilins are: phycoerythrobilin, the typical phycoerythrin acceptor chromophore. Phycoerythrobilin is a linear tetrapyrrole molecule found in cyanobacteria, red algae, and cryptomonads. Together with other bilins such as phycocyanobilin it serves as a light-harvesting pigment in the photosynthetic light-harvesting structures of cyanobacteria called phycobilisomes. Phycoerythrins are composed of (αβ) monomers, usually organised in a disk-shaped trimer (αβ)3 or hexamer (αβ)6 (second ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phycoerythrocyanin
Phycoerythrocyanin is a kind of phycobiliprotein, magenta chromoprotein involved in photosynthesis of some Cyanobacteria. This chromoprotein consists of alpha- and beta-subunits, generally aggregated as hexamer. Alpha-phycoerythrocyanin contains a phycoviolobilin, a violet bilin, that covalently attached at Cys-84, and beta-phycoerythrocyanin contains two phycocyanobilins, a blue bilin, that covalently attached at Cys-84 and -155, respectively. Phycoerythrocyanin is similar to phycocyanin, an important component of the light-harvesting complex (phycobilisome) of cyanobacteria and red algae. While only phycocyanobilin is covalently bound to phycocyanin, leading to an absorption maximum around 620 nm, phycoerythrocyanin containing both phycoviolobilin and phycocyanobilin leads to an absorption maximum around 575 nm. As both phycoerythrocyanin and phycocyanin have phycocyanobilin acting as the terminal acceptor of energy transfer, they fluoresce around 635 nm, which is absorbed by allop ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phycobilisome
Phycobilisomes are light harvesting antennae of photosystem II in cyanobacteria, red algae and glaucophytes. It was lost in the plastids of green algae / plants (chloroplasts). General structure Phycobilisomes are protein complexes (up to 600 polypeptides) anchored to thylakoid membranes. They are made of stacks of chromophorylated proteins, the phycobiliproteins, and their associated linker polypeptides. Each phycobilisome consists of a core made of allophycocyanin, from which several outwardly oriented rods made of stacked disks of phycocyanin and (if present) phycoerythrin(s) or phycoerythrocyanin. The spectral property of phycobiliproteins are mainly dictated by their prosthetic groups, which are linear tetrapyrroles known as phycobilins including phycocyanobilin, phycoerythrobilin, phycourobilin and phycobiliviolin. The spectral properties of a given phycobilin is influenced by its protein environment. Function Each phycobiliprotein has a specific absorption and f ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microscopy
Microscopy is the technical field of using microscopes to view objects and areas of objects that cannot be seen with the naked eye (objects that are not within the resolution range of the normal eye). There are three well-known branches of microscopy: optical, electron, and scanning probe microscopy, along with the emerging field of X-ray microscopy. Optical microscopy and electron microscopy involve the diffraction, reflection, or refraction of electromagnetic radiation/electron beams interacting with the specimen, and the collection of the scattered radiation or another signal in order to create an image. This process may be carried out by wide-field irradiation of the sample (for example standard light microscopy and transmission electron microscopy) or by scanning a fine beam over the sample (for example confocal laser scanning microscopy and scanning electron microscopy). Scanning probe microscopy involves the interaction of a scanning probe with the surface of the objec ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fluorescent Proteins
Fluorescence is the emission of light by a substance that has absorbed light or other electromagnetic radiation. It is a form of luminescence. In most cases, the emitted light has a longer wavelength, and therefore a lower photon energy, than the absorbed radiation. A perceptible example of fluorescence occurs when the absorbed radiation is in the ultraviolet region of the electromagnetic spectrum (invisible to the human eye), while the emitted light is in the visible region; this gives the fluorescent substance a distinct color that can only be seen when the substance has been exposed to UV light. Fluorescent materials cease to glow nearly immediately when the radiation source stops, unlike phosphorescent materials, which continue to emit light for some time after. Fluorescence has many practical applications, including mineralogy, gemology, medicine, chemical sensors ( fluorescence spectroscopy), fluorescent labelling, dyes, biological detectors, cosmic-ray d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Red Algae
Red algae, or Rhodophyta (, ; ), are one of the oldest groups of eukaryotic algae. The Rhodophyta also comprises one of the largest phyla of algae, containing over 7,000 currently recognized species with taxonomic revisions ongoing. The majority of species (6,793) are found in the Florideophyceae (class), and mostly consist of multicellular, marine algae, including many notable seaweeds. Red algae are abundant in marine habitats but relatively rare in freshwaters. Approximately 5% of red algae species occur in freshwater environments, with greater concentrations found in warmer areas. Except for two coastal cave dwelling species in the asexual class Cyanidiophyceae, there are no terrestrial species, which may be due to an evolutionary bottleneck in which the last common ancestor lost about 25% of its core genes and much of its evolutionary plasticity. The red algae form a distinct group characterized by having eukaryotic cells without flagella and centrioles, chloroplasts that l ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photosynthetic Pigments
A photosynthetic pigment (accessory pigment; chloroplast pigment; antenna pigment) is a pigment that is present in chloroplasts or photosynthetic bacteria and captures the light energy necessary for photosynthesis. List of photosynthetic pigments (in order of increasing polarity): *Carotene: an orange pigment *Xanthophyll: a yellow pigment * Phaeophytin ''a'': + energy n the other side of the membr ... when exposed to light. References {{reflist ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Europium
Europium is a chemical element with the symbol Eu and atomic number 63. Europium is the most reactive lanthanide by far, having to be stored under an inert fluid to protect it from atmospheric oxygen or moisture. Europium is also the softest lanthanide, as it can be dented with a fingernail and easily cut with a knife. When oxidation is removed a shiny-white metal is visible. Europium was isolated in 1901 and is named after the continent of Europe. Being a typical member of the lanthanide series, europium usually assumes the oxidation state +3, but the oxidation state +2 is also common. All europium compounds with oxidation state +2 are slightly reducing. Europium has no significant biological role and is relatively non-toxic as compared to other heavy metals. Most applications of europium exploit the phosphorescence of europium compounds. Europium is one of the rarest of the rare-earth elements on Earth.Stwertka, Albert. ''A Guide to the Elements'', Oxford University Press, 1996, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
