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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 metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in fat cells. [5] Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation. Proteins can denature in environmental conditions the protein is not made for. [6]

  4. Glucansucrase - Wikipedia

    en.wikipedia.org/wiki/Glucansucrase

    The two enzymes have similar folding patterns and protein domains. In fact, past attempts to produce drugs targeting glucansucrase have not been successful because the drugs also disrupted amylase, which is necessary to break down starches. [12] [13] This occurred because the active sites of the two enzymes are nearly the same. Glucansucrase ...

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes are not rigid, static structures; instead they have complex internal dynamic motions – that is, movements of parts of the enzyme's structure such as individual amino acid residues, groups of residues forming a protein loop or unit of secondary structure, or even an entire protein domain.

  6. Lactase - Wikipedia

    en.wikipedia.org/wiki/Lactase

    Elimination of specific hydroxyl groups on the glucopyranose moiety does not eliminate catalysis. [17] Lactase also catalyzes the conversion of phlorizin to phloretin and glucose. Lactase (Lactaid commercially) is used as a medication for lactose intolerance. Since it is an enzyme, its function can be inhibited by the acidity of the stomach.

  7. Pepsin - Wikipedia

    en.wikipedia.org/wiki/Pepsin

    Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0. [11] [15] Therefore, pepsin in solutions of up to pH 8.0 can be reactivated upon re-acidification. The stability of pepsin at high pH has significant implications on disease attributed to laryngopharyngeal reflux. Pepsin ...

  8. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The carbohydrate may be in the form of a monosaccharide, disaccharide(s), oligosaccharide(s), polysaccharide(s), or their derivatives (e.g. sulfo- or phospho-substituted). One, a few, or many carbohydrate units may be present. Proteoglycans are a subclass of glycoproteins in which the carbohydrate units are polysaccharides that contain amino ...

  9. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    Maltase breaks maltose into two units of glucose. Findings from that experiment allowed for the divergence of non-competitive and competitive inhibition. Non-competitive inhibition affects the k cat value (but not the K m) on any given graph; this inhibitor binds to a site that has specificity for the certain molecule. Michaelis determined that ...