Denaturation (biochemistry) in the context of "Transmembrane protein"

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⭐ Core Definition: Denaturation (biochemistry)

In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation, radiation, or heat. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Protein denaturation is also a consequence of cell death. Denatured proteins can exhibit a wide range of characteristics, from conformational change and loss of solubility or dissociation of cofactors to aggregation due to the exposure of hydrophobic groups. The loss of solubility as a result of denaturation is called coagulation. When denatured, proteins, e.g., metalloenzymes, lose their 3D structure or metal cofactor and, therefore, cannot function.

Proper protein folding is key to whether a globular or membrane protein can do its job correctly; it must be folded into the native shape to function. However, hydrogen bonds and cofactor-protein binding, which play a crucial role in folding, are rather weak, and thus, easily affected by heat, acidity, varying salt concentrations, chelating agents, and other stressors which can denature the protein. This is one reason why cellular homeostasis is physiologically necessary in most life forms.

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👉 Denaturation (biochemistry) in the context of Transmembrane protein

A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents.

The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-pass membrane proteins, or as multipass membrane proteins. Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, but do not pass through it.

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Denaturation (biochemistry) in the context of Poikilotherm

A poikilotherm (/ˈpɔɪkələˌθɜːrm, pɔɪˈkɪləˌθɜːrm/) is an animal (Greek poikilos – 'various', 'spotted', and therme – 'heat') whose internal temperature varies considerably. Poikilotherms have to survive and adapt to environmental stress. One of the most important stressors is outer environment temperature change, which can lead to alterations in membrane lipid order and can cause protein unfolding and denaturation at elevated temperatures. Poikilotherm is the opposite of homeotherm – an animal which maintains thermal homeostasis. In principle, the term could be applied to any organism, but it is generally only applied to vertebrate animals. Usually the fluctuations are a consequence of variation in the ambient environmental temperature. Many terrestrial ectotherms are poikilothermic. However some ectotherms seek constant-temperature environments to the point that they are able to maintain a constant internal temperature, and are considered actual or practical homeotherms. It is this distinction that often makes the term poikilotherm more useful than the vernacular "cold-blooded", which is sometimes used to refer to ectotherms more generally.

Poikilothermic animals include types of vertebrate animals, specifically some fish, amphibians, and reptiles, as well as many invertebrate animals. The naked mole-rat and sloths are some of the rare mammals which are poikilothermic.

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Denaturation (biochemistry) in the context of Integral membrane protein

An integral, or intrinsic, membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins can be classified as IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents.

Proteins that adhere only temporarily to cellular membranes are known as peripheral membrane proteins. These proteins can either associate with integral membrane proteins, or independently insert in the lipid bilayer in several ways.

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Denaturation (biochemistry) in the context of Coagulation (milk)

Curd is obtained by coagulating milk in a sequential process called curdling. It can be a final dairy product or the first stage in cheesemaking. The coagulation can be caused by adding rennet, a culture, or any edible acidic substance such as lemon juice or vinegar, and then allowing it to coagulate. The increased acidity causes the milk proteins (casein) to tangle into solid masses, or curds. Milk that has been left to sour (raw milk alone or pasteurized milk with added lactic acid bacteria) will also naturally produce curds, and sour milk cheeses are produced this way.

Producing cheese curds is one of the first steps in cheesemaking; the curds are pressed and drained to varying amounts for different styles of cheese and different secondary agents (molds for blue cheeses, etc.) are introduced before the desired aging finishes the cheese. The remaining liquid, which contains only whey proteins, is the whey. In cow's milk, 90 percent of the proteins are caseins. Curds can be used in baking or may be consumed as a snack.

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Denaturation (biochemistry) in the context of Meringue

Meringue (/məˈræŋ/ mə-RANG, French: [məʁɛ̃ɡ] ) is a type of dessert or candy, of French origin, traditionally made from whipped eggwhites and sugar, and occasionally an acidic ingredient such as lemon, vinegar, or cream of tartar. A binding agent such as salt, flour, or gelatin may also be added to the eggs. The key to the formation of a good meringue is the formation of stiff peaks by denaturing the protein ovalbumin (a protein in the egg whites) via mechanical shear.

They are light, airy, and sweet confections. Homemade meringues are often chewy and soft with a crisp exterior, while many commercial meringues are crisp throughout. A uniform crisp texture may be achieved at home by baking at a low temperature (80–90 °C or 176–194 °F) for an extended period of up to two hours.

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Denaturation (biochemistry) in the context of Acid–base homeostasis

Acid–base homeostasis is the homeostatic regulation of the pH of the body's extracellular fluid (ECF). The proper balance between the acids and bases (i.e. the pH) in the ECF is crucial for the normal physiology of the body—and for cellular metabolism. The pH of the intracellular fluid and the extracellular fluid need to be maintained at a constant level.

The three dimensional structures of many extracellular proteins, such as the plasma proteins and membrane proteins of the body's cells, are very sensitive to the extracellular pH. Stringent mechanisms therefore exist to maintain the pH within very narrow limits. Outside the acceptable range of pH, proteins are denatured (i.e. their 3D structure is disrupted), causing enzymes and ion channels (among others) to malfunction.

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Denaturation (biochemistry) in the context of Ricotta

Ricotta (Italian: [riˈkɔtta]) is an Italian whey cheese made from sheep, cow, goat, or Italian water buffalo milk whey left over from the production of other cheeses. However, modern ricotta is often made from milk instead of whey. Like other whey cheeses, it is made by coagulating the proteins that remain after the casein has been used to make cheese, notably albumin and globulin.

Ricotta (lit.'recooked' or 'refined') protein can be harvested if the whey is first allowed to become more acidic by additional fermentation (by letting it sit for 12–24 hours at room temperature). Then the acidified whey is heated to near boiling. The combination of low pH and high temperature denatures the protein and causes it to flocculate, forming a fine curd. Once cooled, it is separated by passing the liquid through a fine cloth, leaving the curd behind.

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