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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. 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 ...

  4. Intracellular pH - Wikipedia

    en.wikipedia.org/wiki/Intracellular_pH

    Intracellular pH (pH i) is the measure of the acidity or basicity (i.e., pH) of intracellular fluid. The pH i plays a critical role in membrane transport and other intracellular processes. In an environment with the improper pH i , biological cells may have compromised function.

  5. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Enzyme inhibitors are molecules that reduce or abolish enzyme activity, while enzyme activators are molecules that increase the catalytic rate of enzymes. These interactions can be either reversible (i.e., removal of the inhibitor restores enzyme activity) or irreversible (i.e., the inhibitor permanently inactivates the enzyme).

  6. RuBisCO - Wikipedia

    en.wikipedia.org/wiki/RuBisCo

    The pH and the concentration of magnesium ions in the fluid compartment (in plants, the stroma of the chloroplast) increases in the light. The role of changing pH and magnesium ion levels in the regulation of RuBisCO enzyme activity is discussed below. Once the carbamate is formed, His335 finalizes the activation by returning to its initial ...

  7. Pepsin - Wikipedia

    en.wikipedia.org/wiki/Pepsin

    Pepsin is most active in acidic environments between pH 1.5 to 2.5. [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]

  8. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme structures unfold when heated or exposed to chemical denaturants and this disruption to the structure typically causes a loss of activity. [26] Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as hot springs are prized by ...

  9. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    Homeostatic control can change the P CO 2 and hence the pH of the arterial plasma within a few seconds. [5] The partial pressure of carbon dioxide in the arterial blood is monitored by the central chemoreceptors of the medulla oblongata. [5] [20] These chemoreceptors are sensitive to the levels of carbon dioxide and pH in the cerebrospinal ...