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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 and radiation, or heat. [3]
Denaturation (food), the deliberate addition of an unpleasantly flavored or poisonous substances to food in order to prevent the consumption of the food for various reasons. Adulterant , a substance added to food for deceptive or malicious reasons, for example to cheaply replace legitimate ingredients.
Denaturation (biochemistry), a structural change in macromolecules caused by extreme conditions; Denaturation (fissile materials), transforming fissile materials so that they cannot be used in nuclear weapons; Denaturation (food), intentional adulteration of food or drink rendering it unfit for consumption while remaining suitable for other uses
1 US gallon or 3.785 litres of denatured alcohol in a metal container. Denatured alcohol, also known as methylated spirits, metho, or meths in Australia, Ireland, New Zealand, South Africa, and the United Kingdom, and as denatured rectified spirit, is ethanol that has additives to make it poisonous, bad-tasting, foul-smelling, or nauseating to discourage its recreational consumption.
Aversive agents—primarily bitterants and pungent agents—are often used to produce an unpleasant flavor. For example, the bitterant denatonium might be added to food used in a laboratory, where such food is not intended for human consumption. [1] A poisonous substance may be added as an even more powerful deterrent.
A chaotropic agent is a molecule in water solution that can disrupt the hydrogen bonding network between water molecules (i.e. exerts chaotropic activity). This has an effect on the stability of the native state of other molecules in the solution, mainly macromolecules ( proteins , nucleic acids ) by weakening the hydrophobic effect .
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For example, the "unfolded" bacteriorhodopsin in SDS micelles has four transmembrane α-helices folded, while the rest of the protein is situated at the micelle-water interface and can adopt different types of non-native amphiphilic structures. Free energy differences between such detergent-denatured and native states are similar to stabilities ...