enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.

  3. Monod–Wyman–Changeux model - Wikipedia

    en.wikipedia.org/wiki/Monod–Wyman–Changeux_model

    The best example of a successful application of the model is the regulation of hemoglobin function. Extensions of the model have been proposed for lattices of proteins by various authors. [5] [6] [7] Edelstein argued that the MWC model gave a better account of the data for hemoglobin than the sequential model [3] could do. [8]

  4. Allosteric enzyme - Wikipedia

    en.wikipedia.org/wiki/Allosteric_enzyme

    Long-range allostery is especially important in cell signaling. [3] Allosteric regulation is also particularly important in the cell's ability to adjust enzyme activity. The term allostery comes from the Greek allos (ἄλλος), "other," and stereos (στερεὀς), "solid (object)." This is in reference to the fact that the regulatory site ...

  5. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    Hemoglobin S (α 2 β S 2) – A variant form of hemoglobin found in people with sickle cell disease. There is a variation in the β-chain gene, causing a change in the properties of hemoglobin, which results in sickling of red blood cells. Hemoglobin C (α 2 β C 2) – Another variant due to a variation

  6. Cooperativity - Wikipedia

    en.wikipedia.org/wiki/Cooperativity

    The sigmoidal shape of hemoglobin's oxygen-dissociation curve results from cooperative binding of oxygen to hemoglobin. An example of positive cooperativity is the binding of oxygen to hemoglobin. One oxygen molecule can bind to the ferrous iron of a heme molecule in each of the four chains of a hemoglobin molecule.

  7. Cell membrane - Wikipedia

    en.wikipedia.org/wiki/Cell_membrane

    Illustration of a eukaryotic cell membrane Comparison of a eukaryotic vs. a prokaryotic cell membrane. The cell membrane (also known as the plasma membrane or cytoplasmic membrane, and historically referred to as the plasmalemma) is a biological membrane that separates and protects the interior of a cell from the outside environment (the extracellular space).

  8. Cooperative binding - Wikipedia

    en.wikipedia.org/wiki/Cooperative_binding

    The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:

  9. Allosteric modulator - Wikipedia

    en.wikipedia.org/wiki/Allosteric_modulator

    Some of them, like benzodiazepines or alcohol, function as psychoactive drugs. [1] The site that an allosteric modulator binds to (i.e., an allosteric site) is not the same one to which an endogenous agonist of the receptor would bind (i.e., an orthosteric site). Modulators and agonists can both be called receptor ligands. [2]