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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. 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]

  4. Chemical bond - Wikipedia

    en.wikipedia.org/wiki/Chemical_bond

    Molecules that are formed primarily from non-polar covalent bonds are often immiscible in water or other polar solvents, but much more soluble in non-polar solvents such as hexane. A polar covalent bond is a covalent bond with a significant ionic character. This means that the two shared electrons are closer to one of the atoms than the other ...

  5. 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.

  6. 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 ]

  7. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Initially, the interaction between the active site and the substrate is non-covalent and transient. There are four important types of interaction that hold the substrate in a defined orientation and form an enzyme-substrate complex (ES complex): hydrogen bonds, van der Waals interactions, hydrophobic interactions and electrostatic force ...

  8. Covalent bond - Wikipedia

    en.wikipedia.org/wiki/Covalent_bond

    2, the hydrogen atoms share the two electrons via covalent bonding. [5] Covalency is greatest between atoms of similar electronegativities. Thus, covalent bonding does not necessarily require that the two atoms be of the same elements, only that they be of comparable electronegativity. Covalent bonding that entails the sharing of electrons over ...

  9. 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 ...