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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. Superoxide dismutase - Wikipedia

    en.wikipedia.org/wiki/Superoxide_dismutase

    Superoxide is known to denature enzymes, oxidize lipids, and fragment DNA. [21] SODs catalyze the production of O 2 and H 2 O 2 from superoxide (O − 2), which results in less harmful reactants. When acclimating to increased levels of oxidative stress, SOD concentrations typically increase with the degree of stress conditions.

  4. RuBisCO - Wikipedia

    en.wikipedia.org/wiki/RuBisCo

    RuBisCO is important biologically because it catalyzes the primary chemical reaction by which inorganic carbon enters the biosphere.While many autotrophic bacteria and archaea fix carbon via the reductive acetyl CoA pathway, the 3-hydroxypropionate cycle, or the reverse Krebs cycle, these pathways are relatively small contributors to global carbon fixation compared to that catalyzed by RuBisCO.

  5. Phagolysosome - Wikipedia

    en.wikipedia.org/wiki/Phagolysosome

    Phagolysosomes function by reducing the pH of their internal environment. The phagolysosome becomes increasingly acidic through the action of V-ATPase proton pumps, reaching a pH as low as 4.5-5.0. [3] This acidic environment is essential for the activation of hydrolytic enzymes and the denaturation of microbial proteins.

  6. Chaperonin - Wikipedia

    en.wikipedia.org/wiki/Chaperonin

    Chaperonins undergo large conformational changes during a folding reaction as a function of the enzymatic hydrolysis of ATP as well as binding of substrate proteins and cochaperonins, such as GroES. These conformational changes allow the chaperonin to bind an unfolded or misfolded protein, encapsulate that protein within one of the cavities ...

  7. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    The uncatalysed half-life is several hundred years. Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion.

  8. 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 ...

  9. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    The specific mode of function of chaperones differs based on their target proteins and location. Various approaches have been applied to study the structure, dynamics and functioning of chaperones. Bulk biochemical measurements have informed us on the protein folding efficiency, and prevention of aggregation when chaperones are present during ...