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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. DNA oxidation - Wikipedia

    en.wikipedia.org/wiki/DNA_oxidation

    DNA oxidation is the process of oxidative damage of deoxyribonucleic acid.As described in detail by Burrows et al., [1] 8-oxo-2'-deoxyguanosine (8-oxo-dG) is the most common oxidative lesion observed in duplex DNA because guanine has a lower one-electron reduction potential than the other nucleosides in DNA.

  4. Slipped strand mispairing - Wikipedia

    en.wikipedia.org/wiki/Slipped_strand_mispairing

    The HD gene [8] is found in all human genomes. In the event that a slippage event occurs there can be a large expansion in the tandem repeats of the HD gene. [8] An individual who is not affected by Huntington's disease will have 6-35 tandem repeats at the HD locus. However, an affected individual will have 36- 121 repeats present. [7]

  5. 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:

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in fat cells. [5] Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation. Proteins can denature in environmental conditions the protein is not made for. [6]

  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...

    The schematic diagram indicates the roles of insufficient DNA repair in aging and cancer, and the role of apoptosis in cancer prevention. An excess of naturally occurring DNA damage, due to inherited deficiencies in particular DNA repair enzymes, can cause premature aging or increased risk for cancer (see DNA repair-deficiency disorder).

  9. Cot analysis - Wikipedia

    en.wikipedia.org/wiki/Cot_analysis

    The procedure involves heating a sample of genomic DNA until it denatures into the single stranded-form, and then slowly cooling it, so the strands can pair back together. While the sample is cooling, measurements are taken of how much of the DNA is base paired at each temperature.