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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. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia.

  4. Necrosis - Wikipedia

    en.wikipedia.org/wiki/Necrosis

    Coagulation occurs as a result of protein denaturation, causing albumin to transform into a firm and opaque state. [6] This pattern of necrosis is typically seen in hypoxic (low-oxygen) environments, such as infarction. Coagulative necrosis occurs primarily in tissues such as the kidney, heart and adrenal glands. [6]

  5. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    The most famous example is the hyperchromicity of DNA that occurs when the DNA duplex is denatured. [1] The UV absorption is increased when the two single DNA strands are being separated, either by heat or by addition of denaturant or by increasing the pH level. The opposite, a decrease of absorbance is called hypochromicity.

  6. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    Chemical denaturation [ edit ] In the less extensive technique of equilibrium unfolding , the fractions of folded and unfolded molecules (denoted as p N {\displaystyle p_{N}} and p U {\displaystyle p_{U}} , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the ...

  7. Liquefactive necrosis - Wikipedia

    en.wikipedia.org/wiki/Liquefactive_necrosis

    Often it is associated with focal bacterial or fungal infections, and can also manifest as one of the symptoms of an internal chemical burn. [2] In liquefactive necrosis, the affected cell is completely digested by hydrolytic enzymes , resulting in a soft, circumscribed lesion consisting of pus and the fluid remains of necrotic tissue.

  8. Coagulative necrosis - Wikipedia

    en.wikipedia.org/wiki/Coagulative_necrosis

    Coagulative necrosis is most commonly caused by conditions that do not involve severe trauma, toxins or an acute or chronic immune response.The lack of oxygen (hypoxia) causes cell death in a localized area which is perfused by blood vessels failing to deliver primarily oxygen, but also other important nutrients.

  9. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Post-translational modifications can occur before protein folding or after. Common biological methods of modifying peptide chains after translation include methylation, phosphorylation, and disulfide bond formation. Methylation often occurs to arginine or lysine and involves adding a methyl group to a nitrogen (replacing a hydrogen).