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  2. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Molecular binding occurs in biological complexes (e.g., between pairs or sets of proteins, or between a protein and a small molecule ligand it binds) and also in abiologic chemical systems, e.g. as in cases of coordination polymers and coordination networks such as metal-organic frameworks.

  3. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    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 ]

  4. 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:

  5. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The region of the protein responsible for binding another molecule is known as the binding site and is often a depression or "pocket" on the molecular surface. This binding ability is mediated by the tertiary structure of the protein, which defines the binding site pocket, and by the chemical properties of the surrounding amino acids' side chains.

  6. Binding domain - Wikipedia

    en.wikipedia.org/wiki/Binding_domain

    In molecular biology, binding domain is a protein domain which binds to a specific atom or molecule, such as calcium or DNA. A protein domain is a part of a protein sequence and a tertiary structure that can change or evolve , function, and live by itself independent of the rest of the protein chain. [ 1 ]

  7. 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.

  8. Avidity - Wikipedia

    en.wikipedia.org/wiki/Avidity

    However, because individual binding events increase the likelihood of occurrence of other interactions (i.e., increase the local concentration of each binding partner in proximity to the binding site), avidity should not be thought of as the mere sum of its constituent affinities but as the combined effect of all affinities participating in the ...

  9. Binding protein - Wikipedia

    en.wikipedia.org/wiki/Binding_protein

    In other projects Wikidata item; ... A binding protein is any protein that acts as an agent to bind two or more molecules together. Examples include: DNA-binding ...