Intermolecular force

An intermolecular force (IMF; also secondary force) is the force that mediates interaction between molecules, including the <a href="/facts/Electromagnetism/oAkmALHT">electromagnetic forces of attraction
or repulsion</a> which act between atoms and other types of neighbouring particles (e.g. <a href="/facts/Atom/FoQ4kGN5">atoms</a> or <a href="/facts/Ion/3bePpDna">ions</a>). Intermolecular forces are weak relative to <a href="/facts/Intramolecular_force/f2Wxm1l3">intramolecular forces</a> – the forces which hold a molecule together. For example, the <a href="/facts/Covalent_bond/EzMLf3Pz">covalent bond</a>, involving sharing electron pairs between atoms, is much stronger than the forces present between neighboring molecules. Both sets of forces are essential parts of <a href="/facts/Force_field_(chemistry)/p9u8nVk8">force fields</a> frequently used in <a href="/facts/Molecular_mechanics/6wPpARWP">molecular mechanics</a>.
The first reference to the nature of microscopic forces is found in <a href="/facts/Alexis_Clairaut/mfnHdyIJ">Alexis Clairaut</a>'s work Théorie de la figure de la Terre, published in Paris in 1743. Other scientists who have contributed to the investigation of microscopic forces include: <a href="/facts/Pierre-Simon_Laplace/6ktp0txb">Laplace</a>, <a href="/facts/Carl_Friedrich_Gauss/f4eSMBD7">Gauss</a>, <a href="/facts/James_Clerk_Maxwell/jtYyze61">Maxwell</a>, <a href="/facts/Ludwig_Boltzmann/xDeLroqt">Boltzmann</a> and <a href="/facts/Linus_Pauling/cBNBzs5c">Pauling</a>.
Attractive intermolecular forces are categorized into the following types:

<ul><li><a href="/facts/Hydrogen_bond/85V86IIg">Hydrogen bonding</a></li>
<li>Ion–dipole forces and ion–induced dipole force</li>
<li><a href="/facts/Cation%25E2%2580%2593%25CF%2580_interaction/sQfF4RbH">Cation–π</a>, σ–π and π–π bonding</li>
<li><a href="/facts/Van_der_Waals_force/jyGU8Vh9">Van der Waals forces</a> – <a href="/facts/Keesom_force/xIcFMvL7">Keesom force</a>, <a href="/facts/Debye_force/xIcFMvL7">Debye force</a>, and <a href="/facts/London_dispersion_force/zU842d26">London dispersion force</a></li>
<li>Cation–cation bonding</li>
<li><a href="/facts/Salt_bridge_(protein_and_supramolecular)/cjEeeG9v">Salt bridge (protein and supramolecular)</a></li></ul>
Information on intermolecular forces is obtained by macroscopic measurements of properties like <a href="/facts/Viscosity/QLVfrdCz">viscosity</a>, <a href="/facts/PVT_(physics)/tLILkepz">pressure, volume, temperature</a> (PVT) data. The link to microscopic aspects is given by <a href="/facts/Virial_coefficient/Dnus06Ep">virial coefficients</a> and intermolecular <a href="/facts/Pair_potential/Xhx2Uwen">pair potentials</a>, such as the <a href="/facts/Mie_potential/5wjURUcj">Mie potential</a>, <a href="/facts/Buckingham_potential/9sJwxlan">Buckingham potential</a> or <a href="/facts/Lennard-Jones_potential/yXwcgLmh">Lennard-Jones potential</a>.
In the broadest sense, it can be understood as such interactions between any particles (<a href="/facts/Molecule/N9ljSfFq">molecules</a>, <a href="/facts/Atom/FoQ4kGN5">atoms</a>, <a href="/facts/Ion/3bePpDna">ions</a> and <a href="/facts/Molecular_ion/FcPWAyLm">molecular ions</a>) in which the formation of chemical (that is, ionic, covalent or metallic) bonds does not occur. In other words, these interactions are significantly weaker than <a href="/facts/Covalent_bond/EzMLf3Pz">covalent</a> ones and do not lead to a significant restructuring of the <a href="/facts/Electronic_structure/RuHwQWfp">electronic structure</a> of the interacting particles. (This is only partially true. For example, all <a href="/facts/Enzyme/DSI1Fh7y">enzymatic</a> and <a href="/facts/Catalysis/LPBS7TQC">catalytic reactions</a> begin with a weak intermolecular interaction between a substrate and an <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a> or a molecule with a <a href="/facts/Catalyst%3a_Agents_of_Change/VUlzR7Cr">catalyst</a>, but several such weak interactions with the required spatial configuration of the active center of the enzyme lead to significant restructuring changes the energy state of molecules or substrate, which ultimately leads to the breaking of some and the formation of other covalent chemical bonds. Strictly speaking, all <a href="/facts/Enzyme_catalysis/4a283vgL">enzymatic reactions</a> begin with intermolecular interactions between the <a href="/facts/Substrate_(chemistry)/6MnaV19h">substrate</a> and the enzyme, therefore the importance of these interactions is especially great in <a href="/facts/Biochemistry/fa2pWEBp">biochemistry</a> and <a href="/facts/Molecular_biology/YgqU35ub">molecular biology</a>, and is the basis of <a href="/facts/Enzyme/DSI1Fh7y">enzymology</a>).

Intermolecular force open-in-new

Intermolecular force