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Monod-Wyman-Changeux Model
In biochemistry, the Monod-Wyman-Changeux model (MWC model, also known as the symmetry model) describes allosteric transitions of proteins made up of identical subunits. It was proposed by Jean-Pierre Changeux in his PhD thesis, and described by Jacques Monod, Jeffries Wyman, and Jean-Pierre Changeux. It contrasts with the sequential model. The concept of two distinct symmetric states is the central postulate of the MWC model. The main idea is that regulated proteins, such as many enzymes and receptors, exist in different interconvertible states ''in the absence of any regulator''. The ratio of the different conformational states is determined by thermal equilibrium. This model is defined by the following rules: # An allosteric protein is an oligomer of protomers that are symmetrically related (for hemoglobin, we shall assume, for the sake of algebraic simplicity, that all four subunits are functionally identical). # Each protomer can exist in (at least) two conformational sta ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Allostery
In biochemistry, allosteric regulation (or allosteric control) is the regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site. The site to which the effector binds is termed the ''allosteric site'' or ''regulatory site''. Allosteric sites allow effectors to bind to the protein, often resulting in a conformational change and/or a change in protein dynamics. Effectors that enhance the protein's activity are referred to as ''allosteric activators'', whereas those that decrease the protein's activity are called ''allosteric inhibitors''. Allosteric regulations are a natural example of control loops, such as feedback from downstream products or feedforward from upstream substrates. Long-range allostery is especially important in cell signaling. Allosteric regulation is also particularly important in the cell's ability to adjust enzyme activity. The term ''allostery'' comes from the Ancient Greek ''allos'' (), "other", and ''stereos' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Agonist
An agonist is a chemical that activates a receptor to produce a biological response. Receptors are cellular proteins whose activation causes the cell to modify what it is currently doing. In contrast, an antagonist blocks the action of the agonist, while an inverse agonist causes an action opposite to that of the agonist. Etymology From the Greek αγωνιστής (agōnistēs), contestant; champion; rival < αγων (agōn), contest, combat; exertion, struggle < αγω (agō), I lead, lead towards, conduct; drive Types of agonists can be activated by either endogenous agonists (such as |
Stuart J
Stuart may refer to: Names *Stuart (name), a given name and surname (and list of people with the name) Automobile *Stuart (automobile) Places Australia Generally *Stuart Highway, connecting South Australia and the Northern Territory Northern Territory *Stuart, the former name for Alice Springs (changed 1933) * Stuart Park, an inner city suburb of Darwin * Central Mount Stuart, a mountain peak Queensland *Stuart, Queensland, a suburb of Townsville *Mount Stuart, Queensland, a suburb of Townsville *Mount Stuart (Queensland), a mountain South Australia *Stuart, South Australia, a locality in the Mid Murray Council *Electoral district of Stuart, a state electoral district *Hundred of Stuart, a cadastral unit Canada * Stuart Channel, a strait in the Gulf of Georgia region of British Columbia United Kingdom *Castle Stuart United States * Stuart, Florida *Stuart, Iowa *Stuart, Nebraska *Stuart, Oklahoma *Stuart, Virginia *Stuart Township, Holt County, Nebraska * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemoglobin
Hemoglobin (haemoglobin BrE) (from the Greek word αἷμα, ''haîma'' 'blood' + Latin ''globus'' 'ball, sphere' + ''-in'') (), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein present in red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the respiratory organs (''e.g.'' lungs or gills) to the rest of the body (''i.e.'' tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power functions of an organism in the process called metabolism. A healthy individual human has 12to 20grams of hemoglobin in every 100mL of blood. In mammals, the chromoprotein makes up about 96% of the red blood cells' dry content (by weight), and around 35% of the total content (including water). Hemoglobin has an oxygen-binding capacity of 1.34mL O2 per gram, which increases the total blood oxygen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pharmacology
Pharmacology is a branch of medicine, biology and pharmaceutical sciences concerned with drug or medication action, where a drug may be defined as any artificial, natural, or endogenous (from within the body) molecule which exerts a biochemical or physiological effect on the cell, tissue, organ, or organism (sometimes the word ''pharmacon'' is used as a term to encompass these endogenous and exogenous bioactive species). More specifically, it is the study of the interactions that occur between a living organism and chemicals that affect normal or abnormal biochemical function. If substances have medicinal properties, they are considered pharmaceuticals. The field encompasses drug composition and properties,functions,sources,synthesis and drug design, molecular and cellular mechanisms, organ/systems mechanisms, signal transduction/cellular communication, molecular diagnostics, interactions, chemical biology, therapy, and medical applications and antipathogenic capabilities. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cooperativity
Cooperativity is a phenomenon displayed by systems involving identical or near-identical elements, which act dependently of each other, relative to a hypothetical standard non-interacting system in which the individual elements are acting independently. One manifestation of this is enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is ''apparently'' increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a binding site. For example, when an oxygen atom binds to one of hemoglobin's four binding sites, the affinity to oxygen of the three remaining available binding sites increases; i.e. oxygen is more likely to bind to a hemoglobin bound to one oxygen than to an unbound hemoglobin. This is referred to as cooperative binding. We also see cooperativity in large chain molecules made of many identical (or nearly identical) subunits (such as DNA, proteins, and phospholipids), when su ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sigmoid Function
A sigmoid function is a mathematical function having a characteristic "S"-shaped curve or sigmoid curve. A common example of a sigmoid function is the logistic function shown in the first figure and defined by the formula: :S(x) = \frac = \frac=1-S(-x). Other standard sigmoid functions are given in the Examples section. In some fields, most notably in the context of artificial neural networks, the term "sigmoid function" is used as an alias for the logistic function. Special cases of the sigmoid function include the Gompertz curve (used in modeling systems that saturate at large values of x) and the ogee curve (used in the spillway of some dams). Sigmoid functions have domain of all real numbers, with return (response) value commonly monotonically increasing but could be decreasing. Sigmoid functions most often show a return value (y axis) in the range 0 to 1. Another commonly used range is from −1 to 1. A wide variety of sigmoid functions including the logistic and hype ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gilbert Smithson Adair
Gilbert Smithson Adair FRS (1896–1979) was an early protein scientist who used osmotic pressure measurements to establish that haemoglobin was a tetramer under physiological conditions. This conclusion led him to be the first to identify cooperative binding, in the context of oxygen binding to haemoglobin. Gilbert Smithson Adair was born on 21 September 1896 in Whitehaven, son of Harold and Anna Mary Adair (née Jackson), who were Quakers. Gilbert and his sister Anna were initially taught at home by a governess. Later, Gilbert was taught at the Quaker Bootham School, where he was a boarder. The family, meanwhile had moved to Egremont, where Harold Adair was managing director of Wyndham Mining Company Ltd. an iron ore mine. Adair entered King's College, Cambridge from 1915 to 1917, gaining a first in Natural Sciences. He was soon employed by the Food Investigation Board, a wartime research group set up by the DSIR to determine how to prevent wastage of food, particularly fish ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protomer
In structural biology, a protomer is the structural unit of an oligomeric protein. It is the smallest unit composed of at least two different protein chains that form a larger hetero-oligomer by association of two or more copies of this unit. The term was introduced by Chetverin to make nomenclature in the Na/K-ATPase enzyme unambiguous. This enzyme is composed of two subunits: a large, catalytic α subunit, and a smaller glycoprotein β subunit (plus a proteolipid, called γ-subunit). At the time it was unclear how many of each work together. In addition, when people spoke of a dimer, it was unclear whether they were referring to αβ or to (αβ)2. Chetverin suggested to call αβ a protomer and (αβ)2 a diprotomer. Protomers usually arrange in cyclic symmetry to form closed point group symmetries. In chemistry, a so-called protomer is a molecule which displays tautomerism due to position of a proton. Examples Hemoglobin is a heterotetramer consisting of four subunits (two α ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Receptor (biochemistry)
In biochemistry and pharmacology, receptors are chemical structures, composed of protein, that receive and transduce signals that may be integrated into biological systems. These signals are typically chemical messengers which bind to a receptor and 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. 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. Receptor proteins can be classified by their location. Transmembrane receptors include ligand-gated ion channels, G protein-coupled receptors, and enzyme-linked hormone receptors. Intracellular receptors are those found inside the cell, and include cytoplasmic receptors and nuclear receptors. A molecule that binds to a receptor is called a ligand ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oligomer
In chemistry and biochemistry, an oligomer () is a molecule that consists of a few repeating units which could be derived, actually or conceptually, from smaller molecules, monomers.Quote: ''Oligomer molecule: A molecule of intermediate relative molecular mass, the structure of which essentially comprises a small plurality of units derived, actually or conceptually, from molecules of lower relative molecular mass.'' The name is composed of Greek elements '' oligo-'', "a few" and '' -mer'', "parts". An adjective form is ''oligomeric''. The oligomer concept is contrasted to that of a polymer, which is usually understood to have a large number of units, possibly thousands or millions. However, there is no sharp distinction between these two concepts. One proposed criterion is whether the molecule's properties vary significantly with the removal of one or a few of the units. An oligomer with a specific number of units is referred to by the Greek prefix denoting that number, wi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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