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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. 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 ...

  5. Ribonuclease - Wikipedia

    en.wikipedia.org/wiki/Ribonuclease

    Structure of RNase A. EC 3.1.27.5: RNase A is an RNase that is commonly used in research. RNase A (e.g., bovine pancreatic ribonuclease A: ) is one of the hardiest enzymes in common laboratory usage; one method of isolating it is to boil a crude cellular extract until all enzymes other than RNase A are denatured. It is specific for single ...

  6. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    Enzyme inhibitors play an important role in all cells, since they are generally specific to one enzyme each and serve to control that enzyme's activity. For example, enzymes in a metabolic pathway may be inhibited by molecules produced later in the pathway, thus curtailing the production of molecules that are no longer needed.

  7. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Structure of a proteasome. Its active sites are inside the tube (blue) where proteins are degraded. 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.

  8. Lysis - Wikipedia

    en.wikipedia.org/wiki/Lysis

    Cell lysis is used in laboratories to break open cells and purify or further study their contents. Lysis in the laboratory may be affected by enzymes or detergents or other chaotropic agents . Mechanical disruption of cell membranes, as by repeated freezing and thawing, sonication , pressure, or filtration may also be referred to as lysis.

  9. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    Biosynthesis, i.e., chemical synthesis occurring in biological contexts, is a term most often referring to multi-step, enzyme-catalyzed processes where chemical substances absorbed as nutrients (or previously converted through biosynthesis) serve as enzyme substrates, with conversion by the living organism either into simpler or more complex ...