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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] |
Artificial Photosynthesis
Artificial photosynthesis is a chemical process that biomimics the natural process of photosynthesis to convert sunlight, water, and carbon dioxide into carbohydrates and oxygen. The term artificial photosynthesis is commonly used to refer to any scheme for capturing and storing the energy from sunlight in the chemical bonds of a fuel (a solar fuel). Photocatalytic water splitting converts water into hydrogen and oxygen and is a major research topic of artificial photosynthesis. Light-driven carbon dioxide reduction is another process studied that replicates natural carbon fixation. Research on this topic includes the design and assembly of devices for the direct production of solar fuels, photoelectrochemistry and its application in fuel cells, and the engineering of enzymes and photoautotrophic microorganisms for microbial biofuel and biohydrogen production from sunlight. Overview The photosynthetic reaction can be divided into two half-reactions of oxidation and redu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phycobilin
Phycobilins (from Greek: '' (phykos)'' meaning "alga", and from Latin: ''bilis'' meaning "bile") are light-capturing bilins found in cyanobacteria and in the chloroplasts of red algae, glaucophytes and some cryptomonads (though not in green algae and plants). Most of their molecules consist of a chromophore which makes them coloured. They are unique among the photosynthetic pigments in that they are bonded to certain water-soluble proteins, known as phycobiliproteins. Phycobiliproteins then pass the light energy to chlorophylls for photosynthesis. The phycobilins are especially efficient at absorbing red, orange, yellow, and green light, wavelengths that are not well absorbed by chlorophyll ''a''. Organisms growing in shallow waters tend to contain phycobilins that can capture yellow/red light, while those at greater depth often contain more of the phycobilins that can capture green light, which is relatively more abundant there. The phycobilins fluoresce at a particular wavel ... [...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] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cyanobacteria Proteins
Cyanobacteria (), also known as Cyanophyta, are a phylum of gram-negative bacteria that obtain energy via photosynthesis. The name ''cyanobacteria'' refers to their color (), which similarly forms the basis of cyanobacteria's common name, blue-green algae, although they are not usually scientifically classified as algae. They appear to have originated in a freshwater or terrestrial environment. Sericytochromatia, the proposed name of the paraphyletic and most basal group, is the ancestor of both the non-photosynthetic group Melainabacteria and the photosynthetic cyanobacteria, also called Oxyphotobacteria. Cyanobacteria use photosynthetic pigments, such as carotenoids, phycobilins, and various forms of chlorophyll, which absorb energy from light. Unlike heterotrophic prokaryotes, cyanobacteria have internal membranes. These are flattened sacs called thylakoids where photosynthesis is performed. Phototrophic eukaryotes such as green plants perform photosynthesis in plastids tha ... [...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] |
Förster Resonance Energy Transfer
Förster resonance energy transfer (FRET), fluorescence resonance energy transfer, resonance energy transfer (RET) or electronic energy transfer (EET) is a mechanism describing energy transfer between two light-sensitive molecules ( chromophores). A donor chromophore, initially in its electronic excited state, may transfer energy to an acceptor chromophore through nonradiative dipole–dipole coupling. The efficiency of this energy transfer is inversely proportional to the sixth power of the distance between donor and acceptor, making FRET extremely sensitive to small changes in distance. Measurements of FRET efficiency can be used to determine if two fluorophores are within a certain distance of each other. Such measurements are used as a research tool in fields including biology and chemistry. FRET is analogous to near-field communication, in that the radius of interaction is much smaller than the wavelength of light emitted. In the near-field region, the excited chromophore e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Stokes Shift
__NOTOC__ Stokes shift is the difference (in energy, wavenumber or frequency units) between positions of the band maxima of the absorption and emission spectra (fluorescence and Raman being two examples) of the same electronic transition. It is named after Irish physicist George Gabriel Stokes. Sometimes Stokes shifts are given in wavelength units, but this is less meaningful than energy, wavenumber or frequency units because it depends on the absorption wavelength. For instance, a 50 nm Stokes shift from absorption at 300 nm is larger in terms of energy than a 50 nm Stokes shift from absorption at 600 nm. When a system (be it a molecule or atom) absorbs a photon, it gains energy and enters an excited state. One way for the system to relax is to emit a photon, thus losing its energy (another method would be the loss of energy as translational mode energy (via vibrational-translational or electronic-translational collisional processes with other atoms or molecules)). When the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FluoProbes
The FluoProbes series of fluorescent dyes were developed by Interchim to improve performances of standard fluorophores. They are designed for labeling biomolecules, cells, tissues or beads in advanced fluorescent detection techniques. * FluoProbes dyes are typically used to label proteins or nucleic acids (ultrafast -3 minutes- labeling of antibodies employs Lightning technology). Labeled products can be used for multiparameter detections, life time resolved fluorescence (TRF), polarisation anisotropy fluorescence, FRET, Quenching, FRAP. They are typically used in biotechnology and research applications as fluorescence microscopy, cell biology or molecular biology, as well as infrared imaging. Derivatives with Amine and Carboxyl suit peptide and nucleic acid synthesis, while reactive ones (with succinimidyl, maleimide and hydrazide) suit conjugation by conventional chemistry, while FluoProbes labeled antibodies and cellular probes (i.e. Phalloidin) suit direct use in immun ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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] |
