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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. Denaturation midpoint - Wikipedia

    en.wikipedia.org/wiki/Denaturation_midpoint

    Denaturation midpoint of a protein is defined as the temperature (T m) or concentration of denaturant (C m) at which both the folded and unfolded states are equally populated at equilibrium (assuming two-state protein folding). T m is often determined using a thermal shift assay.

  4. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.

  5. Proteostasis - Wikipedia

    en.wikipedia.org/wiki/Proteostasis

    Proteostasis is the dynamic regulation of a balanced, functional proteome.The proteostasis network includes competing and integrated biological pathways within cells that control the biogenesis, folding, trafficking, and degradation of proteins present within and outside the cell.

  6. Heat stabilization - Wikipedia

    en.wikipedia.org/wiki/Heat_stabilization

    Heat stabilization is an additive-free preservation technology for tissue samples which stops degradation and changes immediately and permanently. Heat stabilization uses rapid conductive heating, under controlled pressure, to generate a fast, homogeneous and irreversible thermal denaturation of proteins, resulting in a complete and permanent elimination of all enzymatic activity that would ...

  7. Heat shock response - Wikipedia

    en.wikipedia.org/wiki/Heat_shock_response

    Heat shock proteins induced by the HSR can help prevent protein aggregation that is associated with common neurodegenerative diseases such as Alzheimer's, Huntington's, or Parkinson's disease. [8] The diagram depicts actions taken when a stress is introduced to the cell. Stress will induce HSF-1 and cause proteins to misfold.

  8. Heat shock protein - Wikipedia

    en.wikipedia.org/wiki/Heat_shock_protein

    The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). [6] HSPs are found in virtually all living organisms, from bacteria to humans. Heat shock proteins are named according to their molecular weight.

  9. 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