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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. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    Hyperchromicity can be used to track the condition of DNA as temperature changes. The transition/melting temperature (T m) is the temperature where the absorbance of UV light is 50% between the maximum and minimum, i.e. where 50% of the DNA is denatured. A ten fold increase of monovalent cation concentration increases the temperature by 16.6 °C.

  4. Denaturation - Wikipedia

    en.wikipedia.org/wiki/Denaturation

    Denaturation may refer to: . 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

  5. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation.

  6. Polyacrylamide gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Polyacrylamide_gel...

    Polyacrylamide gel electrophoresis (PAGE) is a technique widely used in biochemistry, forensic chemistry, genetics, molecular biology and biotechnology to separate biological macromolecules, usually proteins or nucleic acids, according to their electrophoretic mobility. Electrophoretic mobility is a function of the length, conformation, and ...

  7. Egg white - Wikipedia

    en.wikipedia.org/wiki/Egg_white

    These denatured proteins gather together where the air and water meet and create multiple bonds with the other unraveled proteins, and thus become a foam, holding the incorporated air in place; because the proteins consist of amino acids, some are hydrophilic (attracted to water) and some are hydrophobic (repelled by water).

  8. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site , and residues that catalyse a reaction of that substrate, the catalytic site .

  9. Parents Tackle Elderly Gunman as He Allegedly Opens Fire at ...

    www.aol.com/parents-tackle-elderly-gunman...

    An 83-year-old man has been arrested on suspicion of injuring a man when he allegedly opened fire during a high school band competition on Saturday, Feb.1.