enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  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, 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. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated. In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated.

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes (/ ˈ ɛ n z aɪ m z /) are proteins that act as biological catalysts by accelerating chemical reactions.The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products.

  6. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The best-known role of proteins in the cell is as enzymes, which catalyse chemical reactions. Enzymes are usually highly specific and accelerate only one or a few chemical reactions. Enzymes carry out most of the reactions involved in metabolism, as well as manipulating DNA in processes such as DNA replication, DNA repair, and transcription ...

  7. Gluconeogenesis - Wikipedia

    en.wikipedia.org/wiki/Gluconeogenesis

    Global control of gluconeogenesis is mediated by glucagon (released when blood glucose is low); it triggers phosphorylation of enzymes and regulatory proteins by Protein Kinase A (a cyclic AMP regulated kinase) resulting in inhibition of glycolysis and stimulation of gluconeogenesis. Insulin counteracts glucagon by inhibiting gluconeogenesis.

  8. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia.

  9. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    Glycans serve a variety of structural and functional roles in membrane and secreted proteins. [2] The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the O-GlcNAc modification. Aglycosylation is a feature of engineered antibodies to bypass ...