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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. Maillard reaction - Wikipedia

    en.wikipedia.org/wiki/Maillard_reaction

    Maillard reactions also occur in dried fruit [12] and when champagne ages in the bottle. [13] Caramelization is an entirely different process from Maillard browning, though the results of the two processes are sometimes similar to the naked eye (and taste buds). Caramelization may sometimes cause browning in the same foods in which the Maillard ...

  4. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional.

  5. Deprotonation - Wikipedia

    en.wikipedia.org/wiki/Deprotonation

    Deprotonation (or dehydronation) is the removal (transfer) of a proton (or hydron, or hydrogen cation), (H +) from a Brønsted–Lowry acid in an acid–base reaction. [1][2] The species formed is the conjugate base of that acid. The complementary process, when a proton is added (transferred) to a Brønsted–Lowry base, is protonation (or ...

  6. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    Equilibrium unfolding. In biochemistry, equilibrium unfolding is the process of unfolding a protein or RNA molecule by gradually changing its environment, such as by changing the temperature or pressure, pH, adding chemical denaturants, or applying force as with an atomic force microscope tip. [1][2] If the equilibrium was maintained at all ...

  7. 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 ...

  8. Nucleic acid thermodynamics - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_thermodynamics

    Nucleic acid thermodynamics is the study of how temperature affects the nucleic acid structure of double-stranded DNA (dsDNA). The melting temperature (Tm) is defined as the temperature at which half of the DNA strands are in the random coil or single-stranded (ssDNA) state. Tm depends on the length of the DNA molecule and its specific ...

  9. 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.