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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. Temperature gradient gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Temperature_gradient_gel...

    [1] [2] [3] The same equipment can be used for analysis of protein, which was first done by Thomas E. Creighton of the MRC Laboratory of Molecular Biology, Cambridge, England. [4] Similar looking patterns are produced by proteins and nucleic acids, but the fundamental principles are quite different.

  4. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many ...

  5. 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 ...

  6. Nitrate reductase - Wikipedia

    en.wikipedia.org/wiki/Nitrate_reductase

    The very last step of nitrate reductase inactivation is the binding of the 14-3-3 adapter protein, which is initiated by the presence of Mg 2+ and Ca 2+. [14] Higher plants and some algae post-translationally regulate NR by phosphorylation of serine residues and subsequent binding of a 14-3-3 protein. [15]

  7. Shikimate pathway - Wikipedia

    en.wikipedia.org/wiki/Shikimate_pathway

    The fifth enzyme involved is the shikimate kinase, an enzyme that catalyzes the ATP-dependent phosphorylation of shikimate to form shikimate 3-phosphate (shown in the figure below). [1] Shikimate 3-phosphate is then coupled with phosphoenol pyruvate to give 5-enolpyruvylshikimate-3-phosphate via the enzyme 5-enolpyruvylshikimate-3-phosphate ...

  8. My Honest Review Of Starbucks' 2024 Holiday Drink Menu

    www.aol.com/honest-review-starbucks-2024-holiday...

    New Cold Foam Toppings. Along with returning favorite, a.k.a the peppermint chocolate cold foam, Starbucks is adding Gingerbread and Salted Pecan flavors to the roster.

  9. Protease - Wikipedia

    en.wikipedia.org/wiki/Protease

    Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]