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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. Substrate presentation - Wikipedia

    en.wikipedia.org/wiki/Substrate_presentation

    At a macroscopic level, organelles and vesicle can limit access of an enzyme with to substrate. Sequestration can both elevate and reduce the concentration of a protein in proximity to its substrate. When the substrate is present within a lipid raft, sequestration leads to an increased concentration of the protein near the substrate.

  4. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    Non-competitive inhibition is a type of enzyme inhibition where the inhibitor reduces the activity of the enzyme and binds equally well to the enzyme whether or not it has already bound the substrate. [1] This is unlike competitive inhibition, where binding affinity for the substrate in the enzyme is decreased in the presence of an inhibitor.

  5. 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]

  6. 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.

  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. Taq polymerase - Wikipedia

    en.wikipedia.org/wiki/Taq_polymerase

    Presence of certain ions in the reaction vessel also affects specific activity of the enzyme. Small amounts of potassium chloride (KCl) and magnesium ion (Mg 2+) promote Taq's enzymatic activity. Taq polymerase is maximally activated at 50mM KCl, while optimal Mg 2+ concentration is determined by the concentration of nucleoside triphosphates (dNTPs

  9. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    Once the inhibitor is bound to the enzyme, the slope will be affected, as the K m either increases or decreases from the original K m of the reaction. [4] [5] [6] Most competitive inhibitors function by binding reversibly to the active site of the enzyme. [1] As a result, many sources state that this is the defining feature of competitive ...