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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. Pnictogen bond - Wikipedia

    en.wikipedia.org/wiki/Pnictogen_bond

    In chemistry, a pnictogen bond (PnB) is a non-covalent interaction, occurring where there is a net attractive force between an electrophilic region on a 'donor' pnictogen atom (Pn) in a molecule, and a nucleophilic region on an 'acceptor' atom, which may be in the same or another molecule. [1]

  4. 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.

  5. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    In chemistry, a salt bridge is a combination of two non-covalent interactions: hydrogen bonding and ionic bonding (Figure 1). Ion pairing is one of the most important noncovalent forces in chemistry, in biological systems, in different materials and in many applications such as ion pair chromatography .

  6. Hydrogen bond - Wikipedia

    en.wikipedia.org/wiki/Hydrogen_bond

    Theoretically, the bond strength of the hydrogen bonds can be assessed using NCI index, non-covalent interactions index, which allows a visualization of these non-covalent interactions, as its name indicates, using the electron density of the system. [citation needed]

  7. Cation–π interaction - Wikipedia

    en.wikipedia.org/wiki/Cation–π_interaction

    Bonding energies are significant, with solution-phase values falling within the same order of magnitude as hydrogen bonds and salt bridges. Similar to these other non-covalent bonds, cation–π interactions play an important role in nature, particularly in protein structure, molecular recognition and enzyme catalysis. The effect has also been ...

  8. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Irreversible covalent – a chemical bond is formed in which the product is thermodynamically much more stable than the reactants such that the reverse reaction does not take place. Bound molecules are sometimes called a "molecular complex"—the term generally refers to non-covalent associations. [2]

  9. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Protein–protein_interaction

    Non-covalent bonds are usually established during transient interactions by the combination of weaker bonds, such as hydrogen bonds, ionic interactions, Van der Waals forces, or hydrophobic bonds. [ 13 ]