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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. Alcohol dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Alcohol_dehydrogenase

    Drosophila's fitness is elevated by consuming the low concentration of ethanol. Initial exposure to ethanol causes hyperactivity, followed by incoordination and sedation. [22] Further research has shown that the antioxidant alpha-ketoglutarate may be beneficial in reducing the oxidative stress produced by alcohol consumption.

  4. Aqueous two-phase system - Wikipedia

    en.wikipedia.org/wiki/Aqueous_two-phase_system

    It is a common observation that when oil and water are poured into the same container, they separate into two phases or layers, because they are immiscible.In general, aqueous (or water-based) solutions, being polar, are immiscible with non-polar organic solvents (cooking oil, chloroform, toluene, hexane etc.) and form a two-phase system.

  5. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    To maintain this defined three-dimensional structure, proteins rely on various types of interactions between their amino acid residues. If these interactions are interfered with, for example by extreme pH values, high temperature or high ion concentrations, this will cause the enzyme to denature and lose its catalytic activity. [citation needed]

  6. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Nucleic acids are often denatured by including urea in the buffer, while proteins are denatured using sodium dodecyl sulfate, usually as part of the SDS-PAGE process. For full denaturation of proteins, it is also necessary to reduce the covalent disulfide bonds that stabilize their tertiary and quaternary structure , a method called reducing PAGE.

  7. Deuterium-depleted water - Wikipedia

    en.wikipedia.org/wiki/Deuterium-depleted_water

    Deuterium-depleted water (DDW) is water which has a lower concentration of deuterium than occurs naturally at sea level on Earth. DDW is sometimes known as light water or protium water , although " light water " has long referred to ordinary water, specifically in nuclear reactors .

  8. Ammonium sulfate precipitation - Wikipedia

    en.wikipedia.org/wiki/Ammonium_sulfate_precipitation

    Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium (NH + 4) and sulfate (SO 2− 4) in aqueous solutions. [1] Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive.

  9. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    Protein precipitation is widely used in downstream processing of biological products in order to concentrate proteins and purify them from various contaminants. For example, in the biotechnology industry protein precipitation is used to eliminate contaminants commonly contained in blood. [1]