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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

    Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [13] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation rate.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    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 industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.

  5. Q10 (temperature coefficient) - Wikipedia

    en.wikipedia.org/wiki/Q10_(temperature_coefficient)

    The effects of temperature on enzyme activity. Top - increasing temperature increases the rate of reaction (Q 10 coefficient). Middle - the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom - consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.

  6. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    Thus the analysis of denaturation data with this model requires 7 parameters: ,, k, and the slopes and intercepts of the folded and unfolded state baselines. The solvent exchange model (also called the ‘weak binding model’ or ‘selective solvation’) of Schellman invokes the idea of an equilibrium between the water molecules bound to ...

  7. Taq polymerase - Wikipedia

    en.wikipedia.org/wiki/Taq_polymerase

    Shortages of the necessary enzyme have impaired the ability of countries worldwide to produce test kits for the virus. Without Taq polymerase, the disease detection process is much slower and tedious. [25] Despite the advantages of using Taq polymerase in PCR disease detection, the enzyme is not without its shortcomings. Retroviral diseases ...

  8. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Different proteins are degraded at different rates. Abnormal proteins are quickly degraded, whereas the rate of degradation of normal proteins may vary widely depending on their functions. Enzymes at important metabolic control points may be degraded much faster than those enzymes whose activity is largely constant under all physiological ...

  9. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    The enzyme involved in this reaction is called invertase, and it is the enzyme the kinetics of which have been supported by Michaelis and Menten to be revolutionary for the kinetics of other enzymes. While expressing the rate of the reaction studied, they derived an equation that described the rate in a way which suggested that it is mostly ...