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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. 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 ...

  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. Denatured alcohol - Wikipedia

    en.wikipedia.org/wiki/Denatured_alcohol

    A specially denatured alcohol (SDA) is one of many types of denatured alcohol specified under the United States Title 27 of the Code of Federal Regulations Section 21.151. [11] A specially denatured alcohol is a combination of ethanol and another chemical substance, e.g., ethyl acetate in SDA 29, 35, and 35A , added to render the mixture ...

  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. Chaperone (protein) - Wikipedia

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

    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 ...

  8. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Gel electrophoresis is a process where an electric current is applied to DNA samples creating fragments that can be used for comparison between DNA samples. DNA is extracted. Isolation and amplification of DNA. DNA added to the gel wells. Electric current applied to the gel. DNA bands are separated by size.

  9. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    Hyperchromicity is the increase of absorbance (optical density) of a material. 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.