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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. Buffer solution - Wikipedia

    en.wikipedia.org/wiki/Buffer_solution

    If the pH value of a solution rises or falls too much, the effectiveness of an enzyme decreases in a process, known as denaturation, which is usually irreversible. [6] The majority of biological samples that are used in research are kept in a buffer solution, often phosphate buffered saline (PBS) at pH 7.4.

  4. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    The hyperchromic effect is the striking increase in absorbance of DNA upon denaturation. The two strands of DNA are bound together mainly by the stacking interactions, hydrogen bonds and hydrophobic effect between the complementary bases. The hydrogen bond limits the resonance of the aromatic ring so the absorbance of the sample is limited as well.

  5. Melting curve analysis - Wikipedia

    en.wikipedia.org/wiki/Melting_curve_analysis

    Melting curve analysis is an assessment of the dissociation characteristics of double-stranded DNA during heating. As the temperature is raised, the double strand begins to dissociate leading to a rise in the absorbance intensity, hyperchromicity.

  6. 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

  7. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    This adds a negative charge on the R groups and will thus change how the amino acids behave in comparison to their standard counterparts. Disulfide bond formation is the creation of disulfide bridges ( covalent bonds ) between two cysteine amino acids in a chain which adds stability to the folded structure.

  8. Heller's test - Wikipedia

    en.wikipedia.org/wiki/Heller's_test

    Heller's test is a chemical test that shows that strong acids cause the denaturation of precipitated proteins. Concentrated nitric acid is added to a protein solution from the side of the test tube to form two layers. A white ring appears between the two layers if the test is positive. [1]

  9. Denaturation mapping - Wikipedia

    en.wikipedia.org/wiki/Denaturation_mapping

    Denaturation Mapping is a form of optical mapping, first described in 1966. It is used to characterize DNA molecules without the need for amplification or sequencing . It is based on the differences between the melting temperatures of AT-rich and GC-rich regions. [ 1 ]