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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. Trehalase - Wikipedia

    en.wikipedia.org/wiki/Trehalase

    The cytosolic trehalase enzyme, NT, has been purified and characterized extensively from S. cerevisiae. In non-denaturing gels this enzyme protein exhibited a molecular mass of 160 kDa, while in sodium dodecyl sulfate-polyacrylamide gel electrophoresis it showed a mass of 80 kDa. This hydrolase enzyme is specific for trehalose.

  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. Ribonuclease - Wikipedia

    en.wikipedia.org/wiki/Ribonuclease

    Ribonuclease (commonly abbreviated RNase) is a type of nuclease that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes.

  7. 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]

  8. These 89 Appetizers Might Just Be The Best Part Of ... - AOL

    www.aol.com/89-appetizers-might-just-best...

    Pull-apart bread reaches a whole new level, thanks to brie and cranberry sauce. Use your favorite homemade sauce recipes, but store-bought works too if you're short for time.

  9. Alkaline phosphatase - Wikipedia

    en.wikipedia.org/wiki/Alkaline_phosphatase

    The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase) is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found in the periplasmic ...