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2A Peptides
2A peptides are a class of 18–22 amino acid, aa-long peptides, which can induce ribosomal skipping during translation of a recombinant protein, protein in a biological cell. These peptides share a core sequence motif of , and are found in a wide range of Virus classification, viral families. 2A peptides can be introduced artificially to help generate polyproteins from a single Open reading frame, ORF, by causing the ribosome to fail at making a peptide bond, and then resume translation. The members of 2A peptides are named after the virus in which they have been first described. For example, F2A, the first described 2A peptide, is derived from foot-and-mouth disease virus. The name "2A" itself comes from the gene numbering scheme of this virus. These peptides are also known as "self-cleaving" peptides, which is a known misnomer, because the missing peptide bond is never synthesized by the ribosome, and is thus not cleaved. Members Four members of 2A peptides family are frequen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
2A Peptide From FMVD Action - Co-translational Ribosome Skipping
A, or a, is the first Letter (alphabet), letter and the first vowel letter of the Latin alphabet, used in the modern English alphabet, and others worldwide. Its name in English is ''English alphabet#Letter names, a'' (pronounced ), plural ''aes''. It is similar in shape to the Ancient Greek letter alpha, from which it derives. The uppercase version consists of the two slanting sides of a triangle, crossed in the middle by a horizontal bar. The lowercase version is often written in one of two forms: the double-storey and single-storey . The latter is commonly used in handwriting and fonts based on it, especially fonts intended to be read by children, and is also found in italic type. In English, ''English articles, a'' is the indefinite article, with the alternative form ''an''. Name In English, the name of the letter is the ''long A'' sound, pronounced . Its name in most other languages matches the letter's pronunciation in open syllables. History The earliest know ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Porcine Teschovirus
''Teschovirus'' is a genus of viruses in the order ''Picornavirales'', in the family ''Picornaviridae''. Pigs serve as natural hosts. There are two species in this genus, including Porcine teschovirus, which is responsible for the porcine enteroviral encephalomyelitis disease caused in pigs. The genus name comes from this species and the disease it causes: Teschen disease (a severe and fatal form of pig encephalomyelitis), which itself was named for the town Teschen in Poland/Czechoslovakia where the disease was first recognised in 1929. Genome ''Teschovirus'' has a single-stranded, linear, non-segmented RNA genome. The RNA genome is positively sensed meaning that it has the same polarity as the mRNA and no reverse transcription is necessary. The size of the genome is between 7000 and 9000 nucleotides long. In addition the virus genome contains at the 5' end a protein called VPg and the 3' end is polyadenylated. Through translation of the genome a polyprotein is produced. It is ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Recombinant DNA
Recombinant DNA (rDNA) molecules are DNA molecules formed by laboratory methods of genetic recombination (such as molecular cloning) that bring together genetic material from multiple sources, creating sequences that would not otherwise be found in the genome. Recombinant DNA is the general name for a piece of DNA that has been created by combining two or more fragments from different sources. Recombinant DNA is possible because DNA molecules from all organisms share the same chemical structure, differing only in the nucleotide sequence. Recombinant DNA molecules are sometimes called chimeric DNA because they can be made of material from two different species like the mythical chimera. rDNA technology uses palindromic sequences and leads to the production of sticky and blunt ends. The DNA sequences used in the construction of recombinant DNA molecules can originate from any species. For example, plant DNA can be joined to bacterial DNA, or human DNA can be joined with fun ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Internal Ribosome Entry Site
An internal ribosome entry site, abbreviated IRES, is an RNA element that allows for translation initiation in a cap-independent manner, as part of the greater process of protein synthesis. Initiation of eukaryotic translation nearly always occurs at and is dependent on the 5' cap of mRNA molecules, where the translation initiation complex forms and ribosomes engage the mRNA. IRES elements, however, allow ribosomes to engage the mRNA and begin translation independently of the 5' cap. History IRES sequences were first discovered in 1988 in the poliovirus (PV) and encephalomyocarditis virus (EMCV) RNA genomes in the laboratories of Nahum Sonenberg and Eckard Wimmer, respectively. They are described as distinct regions of RNA molecules that are able to recruit the eukaryotic ribosome to the mRNA. This process is also known as cap-independent translation. It has been shown that IRES elements have a distinct secondary or even tertiary structure, but similar structural features at ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fusion Protein
Fusion proteins or chimeric (kī-ˈmir-ik) proteins (literally, made of parts from different sources) are proteins created through the joining of two or more genes that originally coded for separate proteins. Translation of this '' fusion gene'' results in a single or multiple polypeptides with functional properties derived from each of the original proteins. ''Recombinant fusion proteins'' are created artificially by recombinant DNA technology for use in biological research or therapeutics. '' Chimeric'' or ''chimera'' usually designate hybrid proteins made of polypeptides having different functions or physico-chemical patterns. ''Chimeric mutant proteins'' occur naturally when a complex mutation, such as a chromosomal translocation, tandem duplication, or retrotransposition creates a novel coding sequence containing parts of the coding sequences from two different genes. Naturally occurring fusion proteins are commonly found in cancer cells, where they may function as oncop ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proline
Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the protonated form (NH2+) under biological conditions, while the carboxyl group is in the deprotonated −COO− form. The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG). Proline is the only proteinogenic amino acid which is a secondary amine, as the nitrogen atom is attached both to the α-carbon and to a chain of three carbons that together form a five-membered ring. History and etymology Proline was first isolated in 1900 by Richard Willstätter who obtained the amino a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine disrupts the formation of alpha-helices in secondary protein structure. Its small side chain causes it to favor random coils instead. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a '' Clostridium tetani'' infection) can cause spastic paralysis due to uninhibited muscle contraction. It is the only achiral proteinogenic amino acid. It can fit into both hydrophilic and hydrophobic environments, due to its minimal side chain of only one hydrogen atom. History and etymology Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid. He originally called it "sugar of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide Bond
In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino acid and N2 (nitrogen number two) of another, along a peptide or protein chain. It can also be called a eupeptide bond to distinguish it from an isopeptide bond, which is another type of amide bond between two amino acids. Synthesis When two amino acids form a '' dipeptide'' through a ''peptide bond'', it is a type of condensation reaction. In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other. One loses a hydrogen and oxygen from its carboxyl group (COOH) and the other loses a hydrogen from its amino group (NH2). This reaction produces a molecule of water (H2O) and two amino acids joined by a peptide bond (−CO−NH−). The two joined amino acids are called a dipeptide. The ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serine
Serine (symbol Ser or S) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated − form under biological conditions), a carboxyl group (which is in the deprotonated − form under biological conditions), and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC. Occurrence This compound is one of the proteinogenic amino acids. Only the L- stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865 by Emil Cramer. Its name is derived from the Latin for silk, '' sericum''. Serine's structure was established in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine disrupts the formation of alpha-helices in secondary protein structure. Its small side chain causes it to favor random coils instead. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a '' Clostridium tetani'' infection) can cause spastic paralysis due to uninhibited muscle contraction. It is the only achiral proteinogenic amino acid. It can fit into both hydrophilic and hydrophobic environments, due to its minimal side chain of only one hydrogen atom. History and etymology Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid. He originally called it "sugar of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Permutotetraviridae
''Permutotetraviridae'' is a family of viruses. Lepidopteran insects serve as natural hosts. The family contains one genus that has two species. Diseases associated with this family include: infection outcome varies from unapparent to lethal. Taxonomy ''Permutotetraviridae'' has one genus which contains two species: * Genus: ''Alphapermutotetravirus'' ** '' Euprosterna elaeasa virus'' ** ''Thosea asigna virus ''Thosea'' is a genus of moths of the family Limacodidae The Limacodidae or Eucleidae are a family of moths in the superfamily Zygaenoidea or the Cossoidea;Scoble, M.J. (1992). ''The Lepidoptera: Form, Function and Diversity.'' Oxford Unive ...'' Structure Viruses in ''Permutotetraviridae'' are non-enveloped, with icosahedral geometries, and T=4 symmetry. The diameter is around 40 nm. Genomes are linear, around 5.6kb in length. Life cycle Viral replication is cytoplasmic. Entry into the host cell is achieved by penetration into the host cell. Replication f ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aphthovirus
''Aphthovirus'' (from the Greek , , 'vesicles in the mouth') is a viral genus of the family ''Picornaviridae''. Aphthoviruses infect split-hooved animals, and include the causative agent of foot-and-mouth disease, foot-and-mouth disease virus (FMDV). There are seven FMDV serotypes: A, O, C, SAT 1, SAT 2, SAT 3 and Asia 1, and four non-FMDV serotypes belonging to three additional species Bovine rhinitis A virus (BRAV), Bovine rhinitis B virus (BRBV) and Equine rhinitis A virus (ERAV). Taxonomy The genus contains the following species, listed by scientific name: * ''Aphthovirus bogeli'', Bovine rhinitis A virus * ''Aphthovirus burrowsi'', Equine rhinitis A virus * ''Aphthovirus reedi'', Bovine rhinitis B virus * ''Aphthovirus vesiculae'', Foot-and-mouth disease virus Structure Aphthoviruses are non-enveloped and have an icosahedral capsid with a diameter of around 27 to 30 nm. The assembled viral capsid contains a single copy of the RNA genome and 60 copies of the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
