When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    At the regulatory site, the binding of a ligand may elicit amplified or inhibited protein function. [ 4 ] [ 22 ] The binding of a ligand to an allosteric site of a multimeric enzyme often induces positive cooperativity, that is the binding of one substrate induces a favorable conformation change and increases the enzyme's likelihood to bind to ...

  3. 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:

  4. Cooperativity - Wikipedia

    en.wikipedia.org/wiki/Cooperativity

    One manifestation of this is enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is apparently increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a binding site. For example, when an oxygen atom binds to one of hemoglobin's four binding ...

  5. Ligand (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Ligand_(biochemistry)

    In DNA-ligand binding studies, the ligand can be a small molecule, ion, [1] or protein [2] which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure. Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces.

  6. Ligand - Wikipedia

    en.wikipedia.org/wiki/Ligand

    Cobalt complex HCo(CO) 4 with five ligands. In coordination chemistry, a ligand [a] is an ion or molecule with a functional group that binds to a central metal atom to form a coordination complex. The bonding with the metal generally involves formal donation of one or more of the ligand's electron pairs, often through Lewis bases. [1]

  7. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Among the tightest known protein–protein complexes is that between the enzyme angiogenin and ribonuclease inhibitor; the dissociation constant for the human proteins is 5x10 −16 mol/L. [3] [4] Another biological example is the binding protein streptavidin, which has extraordinarily high affinity for biotin (vitamin B7/H, dissociation ...

  8. Cis effect - Wikipedia

    en.wikipedia.org/wiki/Cis_effect

    CO is a well-known strong pi-accepting ligand in organometallic chemistry that will labilize in the cis position when adjacent to ligands due to steric and electronic effects. The system most often studied for the cis effect is an octahedral complex M(CO) 5 X where X is the ligand that will labilize a CO ligand cis to it.

  9. Binding constant - Wikipedia

    en.wikipedia.org/wiki/Binding_constant

    It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL. The reaction is characterized by the on-rate constant k on and the off-rate constant k off, which have units of M −1 s −1 and s −1, respectively. In equilibrium, the forward binding transition R + L → ...