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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/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 and radiation, or heat. [3]

  3. Bitterant - Wikipedia

    en.wikipedia.org/wiki/Bitterant

    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.

  4. Denaturation - Wikipedia

    en.wikipedia.org/wiki/Denaturation

    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

  5. Denaturation (food) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(food)

    Denaturation is the process by which foods or liquids are made unpleasant or dangerous to consume; it is done by adding a substance known as a denaturant. Aversive agents —primarily bitterants and pungent agents —are often used to produce an unpleasant flavor.

  6. Guanidinium chloride - Wikipedia

    en.wikipedia.org/wiki/Guanidinium_chloride

    Petrunkin and Petrunkin (1927, 1928) appear to be the first who studied the binding of GnHCl to gelatin and a mixture of thermally denatured protein from brain extract. . Greenstein (1938, 1939), however, appears to be the first to discover the high denaturing action of guanidinium halides and thiocyanates in following the liberation of sulfhydryl groups in ovalbumin and other proteins as a ...

  7. Transmembrane protein - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_protein

    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 ...

  8. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    The most famous example is the hyperchromicity of DNA that occurs when the DNA duplex is denatured. [1] The UV absorption is increased when the two single DNA strands are being separated, either by heat or by addition of denaturant or by increasing the pH level. The opposite, a decrease of absorbance is called hypochromicity.

  9. Gel electrophoresis of nucleic acids - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis_of...

    Similarly, RNA and single-stranded DNA can be run and visualised by PAGE gels containing denaturing agents such as urea. PAGE gels are widely used in techniques such as DNA foot printing, EMSA and other DNA-protein interaction techniques. The measurement and analysis are mostly done with a specialized gel analysis software.