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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. Cell damage - Wikipedia

    en.wikipedia.org/wiki/Cell_damage

    The most notable components of the cell that are targets of cell damage are the DNA and the cell membrane. DNA damage: In human cells, both normal metabolic activities and environmental factors such as ultraviolet light and other radiations can cause DNA damage, resulting in as many as one million individual molecular lesions per cell per day. [5]

  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. Chaotropic agent - Wikipedia

    en.wikipedia.org/wiki/Chaotropic_agent

    A chaotropic agent is a substance which disrupts the structure of, and denatures, macromolecules such as proteins and nucleic acids (e.g. DNA and RNA).Chaotropic solutes increase the entropy of the system by interfering with intermolecular interactions mediated by non-covalent forces such as hydrogen bonds, van der Waals forces, and hydrophobic effects.

  6. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    Once the mutants have been established, two methods can be employed to calculate the free energy associated with a salt bridge. One method involves the observation of the melting temperature of the wild-type protein versus that of the three mutants. The denaturation can be monitored through a change in circular dichroism. A reduction in melting ...

  7. 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:

  8. Cell death - Wikipedia

    en.wikipedia.org/wiki/Cell_death

    Overview of signal transduction pathways involved in apoptosis. Cell death is the event of a biological cell ceasing to carry out its functions. This may be the result of the natural process of old cells dying and being replaced by new ones, as in programmed cell death, or may result from factors such as diseases, localized injury, or the death of the organism of which the cells are part.

  9. Mitochondrial outer membrane permeabilization - Wikipedia

    en.wikipedia.org/wiki/Mitochondrial_outer...

    Mitochondrial outer membrane permeabilization (MOMP), also known as the mitochondrial outer membrane permeability, is one of two ways apoptosis (a type of programmed cell death) can be activated. [1] It is part of the intrinsic pathway of apoptosis, also known as the mitochondrial pathway. MOMP is known as the point of no return in apoptosis.