Eos (protein)
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Eos (protein)
EosFP is a photoactivatable green to red fluorescent protein. Its green fluorescence (516 nm) switches to red (581 nm) upon UV irradiation of ~390 nm (violet/blue light) due to a photo-induced modification resulting from a break in the peptide backbone near the chromophore. Eos was first discovered as a tetrameric protein in the stony coral '' Lobophyllia hemprichii''''.'' Like other fluorescent proteins, Eos allows for applications such as the tracking of fusion proteins, multicolour labelling and tracking of cell movement. Several variants of Eos have been engineered for use in specific study systems including mEos2, mEos4 and CaMPARI. History EosFP was first discovered in 2005 during a large scale screen for PAFPs (photoactivatable fluorescent proteins) within the stony coral '' Lobophyllia hemprichii.'' It has since been successfully cloned in ''Escherichia coli'' and fusion constructs have been developed for use in human cells. Eos was named after the Gr ...
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Photoactivatable Fluorescent Protein
Photoactivatable fluorescent proteins (PAFPs) is a type of fluorescent protein that exhibit fluorescence that can be modified by a light-induced chemical reaction. History The first PAFP, Kaede (protein), was isolated from '' Trachyphyllia geoffroyi'' in a cDNA library screen designed to identify new fluorescent proteins. A fluorescent green protein derived from this screen was serendipitously discovered to have sensitivity to ultraviolet light-- We happened to leave one of the protein aliquots on the laboratory bench overnight. The next day, we found that the protein sample on the bench had turned red, whereas the others that were kept in a paper box remained green. Although the sky had been partly cloudy, the red sample had been exposed to sunlight through the south-facing windows. Properties Many PAFPs have been engineered from existing fluorescent proteins or identified from large-scale screens in the wake of Kaede's discovery. Many of these undergo green-to-red ph ...
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Endoplasmic Reticulum
The endoplasmic reticulum (ER) is, in essence, the transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa. The two types of ER share many of the same proteins and engage in certain common activities such as the synthesis of certain lipids and cholesterol. Different types of cells contain different ratios of the two types of ER depending on the activities of the cell. RER is found mainly toward the nucleus of cell and SER towards the cell membrane or plasma ...
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Kaede (protein)
Kaede is a photoactivatable fluorescent protein naturally originated from a stony coral, '' Trachyphyllia geoffroyi''. Its name means "maple" in Japanese. With the irradiation of ultraviolet light (350–400 nm), Kaede undergoes irreversible photoconversion from green fluorescence to red fluorescence. Kaede is a homotetrameric protein with the size of 116 kDa. The tetrameric structure was deduced as its primary structure is only 28 kDa. This tetramerization possibly makes Kaede have a low tendency to form aggregates when fused to other proteins. Discovery The property of photoconverted fluorescence Kaede protein was serendipitously discovered and first reported by Ando et al. in Proceedings of the United States National Academy of Sciences. An aliquot of Kaede protein was discovered to emit red fluorescence after being left on the bench and exposed to sunlight. Subsequent verification revealed that Kaede, which is originally green fluorescent, after exposure to UV light i ...
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Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life ...
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Green Form Cis
Green is the color between cyan and yellow on the visible spectrum. It is evoked by light which has a dominant wavelength of roughly 495570 nm. In subtractive color systems, used in painting and color printing, it is created by a combination of yellow and cyan; in the RGB color model, used on television and computer screens, it is one of the additive primary colors, along with red and blue, which are mixed in different combinations to create all other colors. By far the largest contributor to green in nature is chlorophyll, the chemical by which plants photosynthesize and convert sunlight into chemical energy. Many creatures have adapted to their green environments by taking on a green hue themselves as camouflage. Several minerals have a green color, including the emerald, which is colored green by its chromium content. During post-classical and early modern Europe, green was the color commonly associated with wealth, merchants, bankers, and the gentry, while red was r ...
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