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  2. Non-covalent interaction - Wikipedia

    en.wikipedia.org/wiki/Non-covalent_interaction

    Hydrogen-bonding-in-water. A hydrogen bond (H-bond), is a specific type of interaction that involves dipole–dipole attraction between a partially positive hydrogen atom and a highly electronegative, partially negative oxygen, nitrogen, sulfur, or fluorine atom (not covalently bound to said hydrogen atom).

  3. 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 ...

  4. Chemical polarity - Wikipedia

    en.wikipedia.org/wiki/Chemical_polarity

    The terms "polar" and "nonpolar" are usually applied to covalent bonds, that is, bonds where the polarity is not complete. To determine the polarity of a covalent bond using numerical means, the difference between the electronegativity of the atoms is used.

  5. Covalent bond - Wikipedia

    en.wikipedia.org/wiki/Covalent_bond

    Covalent bonds are also affected by the electronegativity of the connected atoms which determines the chemical polarity of the bond. Two atoms with equal electronegativity will make nonpolar covalent bonds such as H–H. An unequal relationship creates a polar covalent bond such as with H−Cl.

  6. Protein dimer - Wikipedia

    en.wikipedia.org/wiki/Protein_dimer

    Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. [1] An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO. [2]

  7. 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 .

  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. Bonding in solids - Wikipedia

    en.wikipedia.org/wiki/Bonding_in_solids

    Regarding the organization of covalent bonds, recall that classic molecular solids, as stated above, consist of small, non-polar covalent molecules. The example given, paraffin wax , is a member of a family of hydrocarbon molecules of differing chain lengths, with high-density polyethylene at the long-chain end of the series.