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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. 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.

  4. 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

  5. Helicase - Wikipedia

    en.wikipedia.org/wiki/Helicase

    RecQ is a family of DNA helicase enzymes that are found in various organisms including bacteria, archaea, and eukaryotes (like humans). These enzymes play important roles in DNA metabolism during DNA replication, recombination, and repair. There are five known RecQ helicase proteins in humans: RecQ1, BLM, WRN, RecQ4, and RecQ5.

  6. Cell disruption - Wikipedia

    en.wikipedia.org/wiki/Cell_disruption

    The Microfluidizer method used for cell disruption strongly influences the physicochemical properties of the lysed cell suspension, such as particle size, viscosity, protein yield and enzyme activity. In recent years the Microfluidizer method has gained popularity in cell disruption due to its ease of use and efficiency at disrupting many ...

  7. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    The intracellular degradation of protein may be achieved in two ways—proteolysis in lysosome, or a ubiquitin-dependent process that targets unwanted proteins to proteasome. The autophagy -lysosomal pathway is normally a non-selective process, but it may become selective upon starvation whereby proteins with peptide sequence KFERQ or similar ...

  8. Plasmid preparation - Wikipedia

    en.wikipedia.org/wiki/Plasmid_preparation

    The most common method is alkaline lysis, which involves the use of a high concentration of a basic solution, such as sodium hydroxide, to lyse the bacterial cells. [15] [16] [17] When bacteria are lysed under alkaline conditions (pH 12.0–12.5) both chromosomal DNA and protein are denatured; the plasmid DNA however, remains stable.

  9. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    This enables proteins to stay inbound within a cell since the negative phosphorylated site disallows their permeability through the cellular membrane. Protein dephosphorylation allows the cell to replenish phosphates through release of pyrophosphates which saves ATP use in the cell. [55] An example of phosphorylating enzyme is found in E. coli ...