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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. Denitrification - Wikipedia

    en.wikipedia.org/wiki/Denitrification

    Denitrification can lead to a condition called isotopic fractionation in the soil environment. The two stable isotopes of nitrogen, 14 N and 15 N are both found in the sediment profiles. The lighter isotope of nitrogen, 14 N, is preferred during denitrification, leaving the heavier nitrogen isotope, 15 N, in the residual matter.

  4. Denitrifying bacteria - Wikipedia

    en.wikipedia.org/wiki/Denitrifying_bacteria

    This process uses the excess electrons from methane oxidation to reduce nitrates, effectively removing both fixed nitrogen and methane from aquatic systems in habitats ranging from sediment to peat bogs to stratified water columns. [7] The process of anaerobic denitrification may contribute significantly to the global methane and nitrogen ...

  5. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    The hydrophobic patches on the protein surface generate highly ordered water shells. This results in a small decrease in enthalpy, ΔH, and a larger decrease in entropy, ΔS, of the ordered water molecules relative to the molecules in the bulk solution. The overall free energy change, ΔG, of the process is given by the Gibbs free energy equation:

  6. Collagenase - Wikipedia

    en.wikipedia.org/wiki/Collagenase

    In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp, or Lys and at least one other residue is required for catalysis, which may play an electrophillic role.

  7. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Nucleic acids are often denatured by including urea in the buffer, while proteins are denatured using sodium dodecyl sulfate, usually as part of the SDS-PAGE process. For full denaturation of proteins, it is also necessary to reduce the covalent disulfide bonds that stabilize their tertiary and quaternary structure , a method called reducing PAGE.

  8. Hydrolysis - Wikipedia

    en.wikipedia.org/wiki/Hydrolysis

    Usually hydrolysis is a chemical process in which a molecule of water is added to a substance. Sometimes this addition causes both the substance and water molecule to split into two parts. In such reactions, one fragment of the target molecule (or parent molecule) gains a hydrogen ion. It breaks a chemical bond in the compound.

  9. Dephosphorylation - Wikipedia

    en.wikipedia.org/wiki/Dephosphorylation

    Dephosphorylation and its counterpart, phosphorylation, activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides. A notable occurrence of dephosphorylation is the conversion of ATP to ADP and inorganic phosphate. Dephosphorylation employs a type of hydrolytic enzyme, or hydrolase, which cleaves