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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    Note 2: Denaturation can occur when proteins and nucleic acids are subjected to elevated temperature or to extremes of pH, or to nonphysiological concentrations of salt, organic solvents, urea, or other chemical agents. Note 3: An enzyme loses its ability to alter or speed up a chemical reaction when it is denaturized.

  3. 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.

  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

    Equilibrium unfolding. In biochemistry, equilibrium unfolding is the process of unfolding a protein or RNA molecule by gradually changing its environment, such as by changing the temperature or pressure, pH, adding chemical denaturants, or applying force as with an atomic force microscope tip. [1][2] If the equilibrium was maintained at all ...

  6. Pepsin - Wikipedia

    en.wikipedia.org/wiki/Pepsin

    Pepsin / ˈpɛpsɪn / is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site.

  7. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Under certain conditions some proteins can refold; however, in many cases, denaturation is irreversible. [34] Cells sometimes protect their proteins against the denaturing influence of heat with enzymes known as heat shock proteins (a type of chaperone), which assist other proteins both in folding and in remaining folded.

  8. Proteinase K - Wikipedia

    en.wikipedia.org/wiki/Proteinase_K

    It is highly suited to this application since the enzyme is active in the presence of chemicals that denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is used for the destruction of proteins in cell lysates (tissue, cell culture cells) and for ...

  9. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Enzyme activity. Enzyme activity is a measure of the quantity of active enzyme present and is thus dependent on various physical conditions, which should be specified. It is calculated using the following formula: where. = Enzyme activity. = Moles of substrate converted per unit time. = Rate of the reaction. = Reaction volume.