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  2. Binding selectivity - Wikipedia

    en.wikipedia.org/wiki/Binding_selectivity

    Binding selectivity describes how a ligand may bind more preferentially to one receptor than another. A selectivity coefficient is the equilibrium constant for the reaction of displacement by one ligand of another ligand in a complex with the substrate. Binding selectivity is of major importance in biochemistry [1] and in chemical separation ...

  3. Glucose transporter - Wikipedia

    en.wikipedia.org/wiki/Glucose_transporter

    Binding of glucose to one site provokes a conformational change associated with transport, and releases glucose to the other side of the membrane. The inner and outer glucose-binding sites are, it seems, located in transmembrane segments 9, 10, 11; [ 8 ] also, the DLS motif located in the seventh transmembrane segment could be involved in the ...

  4. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    Glucose binds to hexokinase in the active site at the beginning of glycolysis. In biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. [1] The binding partner of the macromolecule is often referred to as a ligand. [2]

  5. Glucose 1-phosphate - Wikipedia

    en.wikipedia.org/wiki/Glucose_1-phosphate

    [1] [2] [3] One reason that cells form glucose 1-phosphate instead of glucose during glycogen breakdown is that the very polar phosphorylated glucose cannot leave the cell membrane and so is marked for intracellular catabolism. Phosphoglucomutase-1 deficiency is known as glycogen storage disease type 14 (GSD XIV). [4]

  6. Receptor–ligand kinetics - Wikipedia

    en.wikipedia.org/wiki/Receptor–ligand_kinetics

    Receptor–ligand binding kinetics also involves the on- and off-rates of binding. A main goal of receptor–ligand kinetics is to determine the concentrations of the various kinetic species (i.e., the states of the receptor and ligand) at all times, from a given set of initial concentrations and a given set of rate constants.

  7. Glycogen phosphorylase - Wikipedia

    en.wikipedia.org/wiki/Glycogen_phosphorylase

    (α-1,4 glycogen chain) n + Pi ⇌ (α-1,4 glycogen chain) n-1 + α-D-glucose-1-phosphate. [2] Glycogen is left with one fewer glucose molecule, and the free glucose molecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphate by the enzyme phosphoglucomutase.

  8. Chemical specificity - Wikipedia

    en.wikipedia.org/wiki/Chemical_specificity

    As the binding process usually leads to a rigidification of both binding partners in the complex, binding of a flexible protein usually comes with an entropic penalty. This is the main reason for the frequently found positive correlation of binding affinity and binding specificity.

  9. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    All cells are coated in either glycoproteins or glycolipids, both of which help determine cell types. [7] Lectins, or proteins that bind carbohydrates, can recognize specific oligosaccharides and provide useful information for cell recognition based on oligosaccharide binding. [citation needed]