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Ovalbumin
Ovalbumin (abbreviated OVA) is the main protein found in egg white, making up approximately 55% of the total protein. Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor. The function of ovalbumin is unknown, although it is presumed to be a storage protein. Research Ovalbumin is an important protein in several different areas of research, including: * general studies of protein structure and properties (because it is available in large quantities). * studies of serpin structure and function (the fact that ovalbumin does not inhibit proteases means that by comparing its structure with that of inhibitory serpins, the structural characteristics required for inhibition can be determined). * proteomics (chicken egg ovalbumin is commonly used as a molecular weight marker for calibrating electrophoresis gels). * immunology (commonly used to stimulate an allergic reaction in test subjects; e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Egg White
Egg white is the clear liquid (also called the albumen or the glair/glaire) contained within an egg. In chickens, it is formed from the layers of secretions of the anterior section of the hen's oviduct during the passage of the egg. It forms around fertilized or unfertilized egg yolks. The primary natural purpose of egg white is to protect the yolk and provide additional nutrition for the growth of the embryo (when fertilized). Egg white consists primarily of about 90% water into which about 10% proteins (including albumins, mucoproteins, and globulins) are dissolved. Unlike the yolk, which is high in lipids (fats), egg white contains almost no fat, and carbohydrate content is less than 1%. Egg whites contain about 56% of the protein in the egg. Egg white has many uses in food (e.g. meringue, mousse) as well as many other uses (e.g. in the preparation of vaccines such as those for influenza). Composition Egg white makes up around two-thirds of a chicken egg by weight. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Egg Allergy
Egg allergy is an immune hypersensitivity to proteins found in chicken eggs, and possibly goose, duck, or turkey eggs. Symptoms can be either rapid or gradual in onset. The latter can take hours to days to appear. The former may include anaphylaxis, a potentially life-threatening condition which requires treatment with Epinephrine (medication), epinephrine. Other presentations may include atopic dermatitis or allergic eosinophilic esophagitis, inflammation of the esophagus. In the United States, 90% of allergic responses to foods are caused by milk, cow's milk, egg (food), eggs, wheat, crustacea, shellfish, peanuts, tree nuts, fish, soy, soybeans, and Sesame, sesame seeds. The declaration of the presence of trace amounts of allergens in foods is not mandatory in any country, with the exception of Brazil. Prevention is by avoiding eating eggs and foods that may contain eggs, such as cake or cookies. It is unclear if the early introduction of the eggs to the diet of babies aged ... [...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 residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 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 pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrophobic
In chemistry, hydrophobicity is the chemical property of a molecule (called a hydrophobe) that is seemingly repelled from a mass of water. In contrast, hydrophiles are attracted to water. Hydrophobic molecules tend to be nonpolar and, thus, prefer other neutral molecules and nonpolar solvents. Because water molecules are polar, hydrophobes do not dissolve well among them. Hydrophobic molecules in water often cluster together, forming micelles. Water on hydrophobic surfaces will exhibit a high contact angle. Examples of hydrophobic molecules include the alkanes, oils, fats, and greasy substances in general. Hydrophobic materials are used for oil removal from water, the management of oil spills, and chemical separation processes to remove non-polar substances from polar compounds. The term ''hydrophobic''—which comes from the Ancient Greek (), "having a fear of water", constructed Liddell, H.G. & Scott, R. (1940). ''A Greek-English Lexicon. revised and augmented ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
β-sheet
The beta sheet (β-sheet, also β-pleated sheet) is a common structural motif, motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone chain, backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of peptide, polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformational isomerism, conformation. The supramolecular association of β-sheets has been implicated in the formation of the Amyloid fibril, fibrils and Amyloid plaques, protein aggregates observed in amyloidosis, Alzheimer's disease and other Proteinopathy, proteinopathies. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Conformational Change
In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors. A macromolecule is usually flexible and dynamic. Its shape can change in response to changes in its environment or other factors; each possible shape is called a conformation, and a transition between them is called a ''conformational change''. Factors that may induce such changes include temperature, pH, voltage, light in chromophores, concentration of ions, phosphorylation, or the binding of a ligand. Transitions between these states occur on a variety of length scales (tenths of Ã… to nm) and time scales (ns to s), and have been linked to functionally relevant phenomena such as allosteric signaling and enzyme catalysis. Laboratory analysis Many biophysical techniques such as crystallography, NMR, electron paramagnetic resonance (EPR) using spin label techniques, circular dichroism (CD), hydrogen exchange, and FRET can be used to study macromo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Signal Peptide
A signal peptide (sometimes referred to as signal sequence, targeting signal, localization signal, localization sequence, transit peptide, leader sequence or leader peptide) is a short peptide (usually 16–30 amino acids long) present at the N-terminus (or occasionally nonclassically at the C-terminus or internally) of most newly synthesized proteins that are destined toward the secretory pathway. These proteins include those that reside either inside certain organelles (the endoplasmic reticulum, Golgi or endosomes), secreted from the cell, or inserted into most cellular membranes. Although most type I membrane-bound proteins have signal peptides, most type II and multi-spanning membrane-bound proteins are targeted to the secretory pathway by their first transmembrane domain, which biochemically resembles a signal sequence except that it is not cleaved. They are a kind of target peptide. Function (translocation) Signal peptides function to prompt a cell to transloc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Journal Of Biological Chemistry
The ''Journal of Biological Chemistry'' (''JBC'') is a weekly peer-reviewed scientific journal that was established in 1905., jbc.org Since 1925, it is published by the American Society for Biochemistry and Molecular Biology. It covers research in areas of biochemistry and molecular biology. The editor is Alex Toker. the journal is fully open access. In press articles are available free on its website immediately after acceptance. Editors The following individuals have served as editors of the journal: * 1906–1909: John Jacob Abel and Christian Archibald Herter * 1909–1910: Christian Archibald Herter * 1910–1914: Alfred Newton Richards * 1914–1925: Donald D. Van Slyke * 1925–1936: Stanley R. Benedict. After Benedict died, John T. Edsall served as temporary editor until the next editor was appointed. * 1937–1958: Rudolph J. Anderson * 1958–1967: John T. Edsall * 1968–1971: William Howard Stein * 1971–2011: Herbert Tabor * 2011–2015: Martha Fedor * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Phosphorylation
Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its function. Approximately 13,000 human proteins have sites that are phosphorylated. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, tyrosine, and histidine. These phosphorylations play important and well-characterized roles in signaling pathways and metabolism. However, other amino acids can also be phosphorylated post-translationally, including arginine, lysine, aspartic acid, glutamic acid and cysteine, a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminal Acetylation
N-terminal acetylation is the protein modification that occurs on the α-amino acid group at the N-termini of proteins. The backbone amino group on the first amino acid (α-amino group) on a protein N-terminus gets an acetyl group (-COCH3) via acetyl-CoA, and this process is catalyzed by enzymes called N-terminal acetyltransferases (NATs).Aksnes, H., N. McTiernan, and T. Arnesen, ''NATs at a glance.'' J Cell Sci, 2023. 136(14). This changes the chemical properties by making the protein more hydrophobic. Adding an acetyl group on the N-terminus of proteins is to date not shown to be reversible. Background Acetylation of a protein is adding an acetyl group on one or several amino acids in the protein. This protein modification can happen internally on an ε- amino acid group of a protein. An internal acetylation is called lysine acetylation, as it is an internal lysine (K) that is added an acetyl group (-COCH3). This process is catalyzed by enzymes named lysine acetyltransferase ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Airway Hyper-responsiveness
Bronchial hyperresponsiveness (or other combinations with airway or hyperreactivity, BH used as a general abbreviation) is a state characterised by easily triggered bronchospasm (contraction of the bronchioles or small airways). Bronchial hyperresponsiveness can be assessed with a bronchial challenge test. This most often uses products like methacholine or histamine. These chemicals trigger bronchospasm in normal individuals as well, but people with bronchial hyperresponsiveness have a lower threshold. Bronchial hyperresponsiveness is a hallmark of asthma but also occurs frequently in people with chronic obstructive pulmonary disease (COPD). In the Lung Health Study, bronchial hyperresponsiveness was present in approximately two-thirds of patients with non-severe COPD, and this predicted lung function decline independently of other factors. In asthma it tends to be reversible with bronchodilator A bronchodilator or broncholytic (although the latter occasionally includes secretor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life. Amino acids can be classified according to the locations of the core structural functional groups ( alpha- , beta- , gamma- amino acids, etc.); other categories relate to polarity, ionization, and side-chain group type ( aliphatic, acyclic, aromatic, polar, 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 on Earth and its emergence. Amino acids are formally named by the IUPAC- IUBMB Joint Commi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
