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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. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    The attraction forces will cause aggregation and precipitation. The pI of most proteins is in the pH range of 4–6. Mineral acids, such as hydrochloric and sulfuric acid are used as precipitants. The greatest disadvantage to isoelectric point precipitation is the irreversible denaturation caused by the mineral acids. For this reason ...

  4. Pasteur effect - Wikipedia

    en.wikipedia.org/wiki/Pasteur_effect

    First, glucose metabolism is faster through ethanol fermentation because it involves fewer enzymes and limits all reactions to the cytoplasm. Second, ethanol has bactericidal activity by causing damage to the cell membrane and protein denaturing , allowing yeast fungus to outcompete environmental bacteria for resources. [ 6 ]

  5. 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.

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many ...

  7. Maillard reaction - Wikipedia

    en.wikipedia.org/wiki/Maillard_reaction

    The crusts of most breads, such as this brioche, are golden-brown mostly as a result of the Maillard reaction.. The Maillard reaction (/ m aɪ ˈ j ɑːr / my-YAR; French:) is a chemical reaction between amino acids and reducing sugars to create melanoidins, the compounds that give browned food its distinctive flavor.

  8. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein.

  9. Protease - Wikipedia

    en.wikipedia.org/wiki/Protease

    Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]