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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. Fungal extracellular enzyme activity - Wikipedia

    en.wikipedia.org/wiki/Fungal_extracellular...

    Benefits of exoenzyme production can also be lost after secretion because the enzymes are liable to denature, degrade or diffuse away from the producer cell. Enzyme production and secretion is an energy intensive process [ 14 ] and, because it consumes resources otherwise available for reproduction, there is evolutionary pressure to conserve ...

  4. 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]

  5. 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.

  6. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Substrate presentation is a process where the enzyme is sequestered away from its substrate. Enzymes can be sequestered to the plasma membrane away from a substrate in the nucleus or cytosol. [54] Or within the membrane, an enzyme can be sequestered into lipid rafts away from its substrate in the disordered region.

  7. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Most enzymes are sensitive to pH and have specific ranges of activity. All have an optimum pH. The pH can stop enzyme activity by denaturating (altering) the three-dimensional shape of the enzyme by breaking ionic, and hydrogen bonds. Most enzymes function between a pH of 6 and 8; however pepsin in the stomach works best at a pH of 2 and ...

  8. Pepsin - Wikipedia

    en.wikipedia.org/wiki/Pepsin

    [11] [12] Accordingly, its primary site of synthesis and activity is in the stomach (pH 1.5 to 2). In humans the concentration of pepsin in the stomach reaches 0.5 – 1 mg/mL. [13] [14] Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0.

  9. Reactive oxygen species production in marine microalgae

    en.wikipedia.org/wiki/Reactive_oxygen_species...

    Reactive oxygen species are present in low concentrations in seawater and are produced primarily through the photolysis of organic and inorganic matter. [12] However, the biological production of ROS, generated through algal photosynthesis and subsequently 'leaked' to the environment, can contribute significantly to concentrations in the water ...