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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. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    Furthermore, one can assess whether the folding proceeds according to a two-state unfolding as described above. This can be done with differential scanning calorimetry by comparing the calorimetric enthalpy of denaturation i.e. the area under the peak, A peak {\displaystyle A_{\text{peak}}} to the van 't Hoff enthalpy described as follows:

  4. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Many allergies are caused by the incorrect folding of some proteins because the immune system does not produce the antibodies for certain protein structures. [5] Denaturation of proteins is a process of transition from a folded to an unfolded state. It happens in cooking, burns, proteinopathies, and other contexts. Residual structure present ...

  5. Slipped strand mispairing - Wikipedia

    en.wikipedia.org/wiki/Slipped_strand_mispairing

    SSM events can result in either insertions or deletions. Insertions are thought to be self-accelerating: as repeats grow longer, the probability of subsequent mispairing events increases. Insertions can expand simple tandem repeats by one or more units. In long repeats, expansions may involve two or more units.

  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. 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.

  8. DNA damage (naturally occurring) - Wikipedia

    en.wikipedia.org/wiki/DNA_damage_(naturally...

    Inflammation-induced ROS that cause DNA damage can trigger apoptosis, [52] [53] but may also cause cancer if repair and apoptotic processes are insufficiently protective. [ 45 ] Bile acids , stored in the gall bladder, are released into the small intestine in response to fat in the diet.

  9. Chevron plot - Wikipedia

    en.wikipedia.org/wiki/Chevron_plot

    A priori information on the Cm of a protein can be obtained from equilibrium experiments. In fitting to a two-state model, the logarithm of the folding and unfolding rates is assumed to depend linearly on the denaturant concentration, thus resulting in the slopes m f and m u , called the folding and unfolding m-values, respectively (also called ...