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  2. Non-covalent interaction - Wikipedia

    en.wikipedia.org/wiki/Non-covalent_interaction

    The chemical energy released in the formation of non-covalent interactions is typically on the order of 1–5 kcal/mol (1000–5000 calories per 6.02 × 10 23 molecules). [2] Non-covalent interactions can be classified into different categories, such as electrostatic, π-effects, van der Waals forces, and hydrophobic effects. [3] [2]

  3. Host–guest chemistry - Wikipedia

    en.wikipedia.org/wiki/Host–guest_chemistry

    Host–guest chemistry encompasses the idea of molecular recognition and interactions through non-covalent bonding. Non-covalent bonding is critical in maintaining the 3D structure of large molecules, such as proteins and is involved in many biological processes in which large molecules bind specifically but transiently to one another.

  4. Supramolecular polymer - Wikipedia

    en.wikipedia.org/wiki/Supramolecular_polymer

    Supramolecular polymers are a subset of polymers where the monomeric units are connected by reversible and highly directional secondary interactions–that is, non-covalent bonds. These non-covalent interactions include van der Waals interactions, hydrogen bonding, Coulomb or ionic interactions, π-π stacking, metal coordination, halogen ...

  5. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Non-covalent – no chemical bonds are formed between the two interacting molecules hence the association is fully reversible Reversible covalent – a chemical bond is formed, however the free energy difference separating the noncovalently-bonded reactants from bonded product is near equilibrium and the activation barrier is relatively low ...

  6. Macromolecular assembly - Wikipedia

    en.wikipedia.org/wiki/Macromolecular_assembly

    MAs of macromolecules are held in their defined forms by non-covalent intermolecular interactions (rather than covalent bonds), and can be in either non-repeating structures (e.g., as in the ribosome (image) and cell membrane architectures), or in repeating linear, circular, spiral, or other patterns (e.g., as in actin filaments and the ...

  7. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Protein–protein_interaction

    Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that ...

  8. Supramolecular chemistry - Wikipedia

    en.wikipedia.org/wiki/Supramolecular_chemistry

    Supramolecular chemistry refers to the branch of chemistry concerning chemical systems composed of a discrete number of molecules.The strength of the forces responsible for spatial organization of the system range from weak intermolecular forces, electrostatic charge, or hydrogen bonding to strong covalent bonding, provided that the electronic coupling strength remains small relative to the ...

  9. Protein–ligand complex - Wikipedia

    en.wikipedia.org/wiki/Protein–ligand_complex

    In non-covalent interactions there is no sharing of electrons like in covalent interactions or bonds. Non-covalent binding may depend on hydrogen bonds , hydrophobic forces , van der Waals forces , π-π interactions , electrostatic interactions in which no electrons are shared between the two or more involved molecules. [ 4 ]