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Hemagglutinin (influenza)
Influenza
Influenza
hemagglutinin (HA) or haemagglutinin (British English) is a glycoprotein found on the surface of influenza viruses. It is responsible for binding the virus to cells with sialic acid on the membranes, such as cells in the upper respiratory tract or erythrocytes.[1] It is also responsible for the fusion of the viral envelope with the endosome membrane, after the pH has been reduced. The name "hemagglutinin" comes from the protein's ability to cause red blood cells (erythrocytes) to clump together ("agglutinate") in vitro.[2]Contents1 Subtypes 2 Function and mechanism 3 Structure 4 Neutralizing antibodies 5 See also 6 References 7 External linksSubtypes[edit]Structure of influenza, showing neuraminidase marked as NA and hemagglutinin as HA.HA has at least 18 different antigens. These subtypes are named H1 through H18
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Pfam
Pfam
Pfam
is a database of protein families that includes their annotations and multiple sequence alignments generated using hidden Markov models.[1][2][3] The most recent version, Pfam
Pfam
31.0, was released in March 2017 and contains 16,712 families.[4]Contents1 Uses 2 Features<
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Cylinder (geometry)
A cylinder (from Greek κύλινδρος – kulindros, "roller, tumbler"[1]), has traditionally been a three-dimensional solid, one of the most basic of curvilinear geometric shapes. It is the idealized version of a solid physical tin can having lids on top and bottom. This traditional view is still used in elementary treatments of geometry, but the advanced mathematical viewpoint has shifted to the infinite curvilinear surface and this is how a cylinder is now defined in various modern branches of geometry and topology. The shift in the basic meaning (solid versus surface) has created some ambiguity with terminology. It is generally hoped that context makes the meaning clear
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InterPro
InterPro is a database of protein families, domains and functional sites in which identifiable features found in known proteins can be applied to new protein sequences[2] in order to functionally characterise them.[3][4] The contents of InterPro consist of diagnostic signatures and the proteins that they significantly match. The signatures consist of models (simple types, such as regular expressions or more complex ones, such as Hidden Markov models) which describe protein families, domains or sites. Models are built from the amino acid sequences of known families or domains and they are subsequently used to search unknown sequences (such as those arising from novel genome sequencing) in order to classify them
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Influenza A Virus Subtype H5n2
H5N2 is a subtype of the species Influenzavirus A
Influenzavirus A
(avian influenza virus or bird flu virus). The subtype infects a wide variety of birds, including chickens, ducks, turkeys, falcons, and ostriches. Affected birds usually do not appear ill, and the disease is often mild as avian influenza viral subtypes go. Some variants of the subtype are much more pathogenic than others, and outbreaks of "high-path" H5N2 result in the culling of thousands of birds in poultry farms from time to time. It appears that people who work with birds can be infected by the virus, but suffer hardly any noticeable health effects. Even people exposed to the highly pathogenic H5N2 variety that killed ostrich chicks in South Africa only seem to have developed conjunctivitis, or a perhaps a mild respiratory illness
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Amino Acid
Amino acids
Amino acids
are organic compounds containing amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R group) specific to each amino acid.[1][2][3] The key elements of an amino acid are carbon (C), hydrogen (H), oxygen (O), and nitrogen (N), although other elements are found in the side chains of certain amino acids. About 500 naturally occurring amino acids are known (though only 20 appear in the genetic code) and can be classified in many ways.[4] They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.)
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Protease
A protease (also called a peptidase or proteinase) is an enzyme that performs proteolysis; protein catabolism by hydrolysis of peptide bonds. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms
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Vertebrate
Fire salamander
Fire salamander
(Amphibia), saltwater crocodile (Reptilia), southern cassowary (Aves), black-and-rufous giant elephant shrew (Mammalia), ocean sunfish (Osteichthyes)Scientific classification Kingdom: AnimaliaPhylum: ChordataClade: CraniataSubphylum: Vertebrata J-B
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Receptor (biochemistry)
In biochemistry and pharmacology, a receptor is a protein molecule that receives chemical signals from outside a cell.[1] When such chemical signals bind to a receptor, they cause some form of cellular/tissue response, e.g. a change in the electrical activity of a cell. There are three main ways the action of the receptor can be classified: relay of signal, amplification, or integration.[2] Relaying sends the signal onward, amplification increases the effect of a single ligand, and integration allows the signal to be incorporated into another biochemical pathway.[2] In this sense, a receptor is a protein-molecule that recognizes and responds to endogenous chemical signals, e.g. an acetylcholine receptor recognizes and responds to its endogenous ligand, acetylcholine. However, sometimes in pharmacology, the term is also used to include other proteins that are drug targets, such as enzymes, transporters, and ion channels. Receptor proteins can be classified by their location
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Lysosome
A lysosome is a membrane-bound organelle found in nearly all animal cells. They are spherical vesicles that contain hydrolytic enzymes that can break down many kinds of biomolecules. Put simply, a lysosome is a type of vesicle with specific composition, of both its membrane proteins, and proteins of its lumen. The lumen's pH (4.5–5.0)[1] is optimal for the enzymes involved in hydrolysis, analogous to the activity of the stomach. Besides degradation of polymers, the lysosome is involved in various cell processes, including secretion, plasma membrane repair, cell signaling, and energy metabolism.[2] The lysosomes also act as the waste disposal system of the cell by digesting unwanted materials in the cytoplasm, both from outside the cell and obsolete components inside the cell. Material from outside the cell is taken-up through endocytosis, while material from the inside of the cell is digested through autophagy
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Fusion Peptide
Membrane fusion proteins (not to be confused with chimeric or fusion proteins) are proteins that cause fusion of biological membranes
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Monomer
A monomer (/ˈmɒnəmər/ MON-ə-mər) (mono-, "one" + -mer, "part") is a molecule that "can undergo polymerization thereby contributing constitutional units to the essential structure of a macromolecule".[1][2] Large numbers of monomers combine to form polymers in a process called polymerization.Contents1 Classification 2 Synthetic monomers 3 Biopolymers 4 Natural monomers4.1 Amino acids 4.2 Nucleotides 4.3 Glucose
Glucose
and related sugars 4.4 Isoprene5 See also 6 Notes 7 External linksClassification[edit] Monomers can be classified in many ways. They can be subdivided into two broad classes, depending on the kind of the polymer that they form. Monomers that participate in condensation polymerization have a different stoichiometry than monomers that participate in addition polymerization:[3]This nylon is formed by condensation polymerization of two monomers, yielding water.Other classifications include:natural vs synthetic monomers, e.g
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Sweden
Coordinates: 63°N 16°E / 63°N 16°E / 63; 16Kingdom of Sweden Konungariket Sverige[a]FlagGreater coat of armsMotto: (royal) "För Sverige – i tiden"[a] "For Sweden
Sweden
– With the Times"[1]Anthem: Du gamla, Du fria[b] Thou ancient, thou freeRoyal anthem: Kungssången Song of the KingLocation of  Sweden  (dark green) – in Europe  (green & dark grey) – in the European Union  (green)  –  [Legend]Capital and largest city Stockholm 59°21′N 18°
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Alpha Helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a righthand-spiral conformation (i.e. helix) in which every backbone N−H group donates a hydrogen bond to the backbone C=O group of the amino acid located three or four residues earlier along the protein sequence. The alpha helix is also called a classic Pauling–Corey–Branson α-helix
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Protein Precursor
A protein precursor, also called a pro-protein or pro-peptide, is an inactive protein (or peptide) that can be turned into an active form by post-translational modification, such as breaking off a piece of the molecule or adding on another molecule. The name of the precursor for a protein is often prefixed by pro-. Examples include proinsulin and proopiomelanocortin, which are both prohormones. Protein
Protein
precursors are often used by an organism when the subsequent protein is potentially harmful, but needs to be available on short notice and/or in large quantities. Enzyme
Enzyme
precursors are called zymogens or proenzymes. Examples are enzymes of the digestive tract in humans. Some protein precursors are secreted from the cell. Many of these are synthesized with an N-terminal signal peptide that targets them for secretion. Like other proteins that contain a signal peptide, their name is prefixed by pre
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Polypeptides
Peptides (from Gr.: πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are short chains of amino acid monomers linked by peptide (amide) bonds. The covalent chemical bonds are formed when the carboxyl group of one amino acid reacts with the amino group of another. The shortest peptides are dipeptides, consisting of 2 amino acids joined by a single peptide bond, followed by tripeptides, tetrapeptides, etc
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