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Heunggongvirae
''Duplodnaviria'' is a realm of viruses that includes all double-stranded DNA viruses that encode the HK97 fold major capsid protein. The HK97 fold major capsid protein (HK97 MCP) is the primary component of the viral capsid, which stores the viral deoxyribonucleic acid (DNA). Viruses in the realm also share a number of other characteristics, such as an icosahedral capsid, an opening in the viral capsid called a portal, a protease enzyme that empties the inside of the capsid prior to DNA packaging, and a terminase enzyme that packages viral DNA into the capsid. ''Duplodnaviria'' was established in 2019 based on the shared characteristics of viruses in the realm. There are two groups of viruses in ''Duplodnaviria'': tailed bacteriophages of the order ''Caudovirales'', which infect prokaryotes, and herpesviruses of the order ''Herpesvirales'', which infect animals. Tailed bacteriophages are very diverse and ubiquitous worldwide, and they may be the oldest lineage of viruses. Herpe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Classification
Classification is a process related to categorization, the process in which ideas and objects are recognized, differentiated and understood. Classification is the grouping of related facts into classes. It may also refer to: Business, organizations, and economics * Classification of customers, for marketing (as in Master data management) or for profitability (e.g. by Activity-based costing) * Classified information, as in legal or government documentation * Job classification, as in job analysis * Standard Industrial Classification, economic activities Mathematics * Attribute-value system, a basic knowledge representation framework * Classification theorems in mathematics * Mathematical classification, grouping mathematical objects based on a property that all those objects share * Statistical classification, identifying to which of a set of categories a new observation belongs, on the basis of a training set of data Media * Classification (literature), a figure of spee ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Latin
Latin (, or , ) is a classical language belonging to the Italic branch of the Indo-European languages. Latin was originally a dialect spoken in the lower Tiber area (then known as Latium) around present-day Rome, but through the power of the Roman Republic it became the dominant language in the Italian region and subsequently throughout the Roman Empire. Even after the fall of Western Rome, Latin remained the common language of international communication, science, scholarship and academia in Europe until well into the 18th century, when other regional vernaculars (including its own descendants, the Romance languages) supplanted it in common academic and political usage, and it eventually became a dead language in the modern linguistic definition. Latin is a highly inflected language, with three distinct genders (masculine, feminine, and neuter), six or seven noun cases (nominative, accusative, genitive, dative, ablative, and vocative), five declensions, four ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Concatemer
A concatemer is a long continuous DNA molecule that contains multiple copies of the same DNA sequence linked in series. These polymeric molecules are usually copies of an entire genome linked end to end and separated by ''cos'' sites (a protein binding nucleotide sequence that occurs once in each copy of the genome). Concatemers are frequently the result of rolling circle replication, and may be seen in the late stage of bacterial infection by phages. As an example, if the genes in the phage DNA are arranged ABC, then in a concatemer the genes would be ABCABCABCABC and so on (assuming synthesis was initiated between genes C and A). They are further broken by ribozymes. During active infection, some species of viruses have been shown to replicate their genetic material via the formation of concatemers. In the case of ''human herpesvirus-6'', its entire genome is made over and over on a single strand. These long concatemers are subsequently cleaved between the pac-1 and pac-2 regio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Viral Replication
Viral replication is the formation of biological viruses during the infection process in the target host cells. Viruses must first get into the cell before viral replication can occur. Through the generation of abundant copies of its genome and packaging these copies, the virus continues infecting new hosts. Replication between viruses is greatly varied and depends on the type of genes involved in them. Most DNA viruses assemble in the nucleus while most RNA viruses develop solely in cytoplasm. Viral production / replication Viruses multiply only in living cells. The host cell must provide the energy and synthetic machinery and the low- molecular-weight precursors for the synthesis of viral proteins and nucleic acids. The virus replication occurs in seven stages, namely; # Attachment # Entry, # Uncoating, # Transcription / mRNA production, # Synthesis of virus components, # Virion assembly and # Release (Liberation Stage). Attachment It is the first step of viral replic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proteolysis
Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes including apoptosis, as well as preventing the accumulation of unwanted or misfolded proteins in cells. Consequently, abnormality in the regulation of proteolysis can cause disease. Proteolysis can also be used as an analytical tool for studying proteins in the laboratory, and it may also be used in industry, for example in food pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protease
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes (increases reaction rate or "speeds up") proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in many biological functions, including digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling. In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Hierarchy of proteases Based on catalytic residue Proteases can be classified into seven broad groups: * Serine prot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
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 Wetlaufe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Scaffold Protein
In biology, scaffold proteins are crucial regulators of many key signalling pathways. Although scaffolds are not strictly defined in function, they are known to interact and/or bind with multiple members of a signalling pathway, tethering them into complexes. In such pathways, they regulate signal transduction and help localize pathway components (organized in complexes) to specific areas of the cell such as the plasma membrane, the cytoplasm, the nucleus, the Golgi, endosomes, and the mitochondria. History The first signaling scaffold protein discovered was the Ste5 protein from the yeast ''Saccharomyces cerevisiae''. Three distinct domains of Ste5 were shown to associate with the protein kinases Ste11, Ste7, and Fus3 to form a multikinase complex. Function Scaffold proteins act in at least four ways: tethering signaling components, localizing these components to specific areas of the cell, regulating signal transduction by coordinating positive and negative feedb ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ribosome
Ribosomes ( ) are macromolecular machines, found within all cells, that perform biological protein synthesis (mRNA translation). Ribosomes link amino acids together in the order specified by the codons of messenger RNA (mRNA) molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA (rRNA) molecules and many ribosomal proteins (RPs or r-proteins). The ribosomes and associated molecules are also known as the ''translational apparatus''. Overview The sequence of DNA that encodes the sequence of the amino acids in a protein is transcribed into a messenger RNA chain. Ribosomes bind to messenger RNAs and use their sequences for determining the correct sequence of amino acids to generate a given protein. Amino acids are selected and carried to the ribosome by transfer RNA, transfer RNA (tRNA) molecules, which enter the ribosome and bind to the messenger RNA chain vi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Synthesis
Protein biosynthesis (or protein synthesis) is a core biological process, occurring inside cells, balancing the loss of cellular proteins (via degradation or export) through the production of new proteins. Proteins perform a number of critical functions as enzymes, structural proteins or hormones. Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences. Protein synthesis can be divided broadly into two phases - transcription and translation. During transcription, a section of DNA encoding a protein, known as a gene, is converted into a template molecule called messenger RNA (mRNA). This conversion is carried out by enzymes, known as RNA polymerases, in the nucleus of the cell. In eukaryotes, this mRNA is initially produced in a premature form (pre-mRNA) which undergoes post-transcriptional modifications to produce mature mRNA. The mature mRNA is exported from the cell nucleus via nuclear pores to the cytoplasm of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Folding
Protein folding is the physical process by which a protein chain is translated to its native three-dimensional structure, typically a "folded" conformation by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA to a linear chain of amino acids. At this stage the polypeptide lacks any stable (long-lasting) three-dimensional structure (the left hand side of the first figure). As the polypeptide chain is being synthesized by a ribosome, the linear chain begins to fold into its three-dimensional structure. Folding of many proteins begins even during translation of the polypeptide chain. Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein (the right hand side of the figure ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Icosahedral
In geometry, an icosahedron ( or ) is a polyhedron with 20 faces. The name comes and . The plural can be either "icosahedra" () or "icosahedrons". There are infinitely many non- similar shapes of icosahedra, some of them being more symmetrical than others. The best known is the (convex, non-stellated) regular icosahedron—one of the Platonic solids—whose faces are 20 equilateral triangles. Regular icosahedra There are two objects, one convex and one nonconvex, that can both be called regular icosahedra. Each has 30 edges and 20 equilateral triangle faces with five meeting at each of its twelve vertices. Both have icosahedral symmetry. The term "regular icosahedron" generally refers to the convex variety, while the nonconvex form is called a ''great icosahedron''. Convex regular icosahedron The convex regular icosahedron is usually referred to simply as the ''regular icosahedron'', one of the five regular Platonic solids, and is represented by its Schläfli symbol , cont ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
