nietcovalente

Nietcovalente interactions are forces that do not involve sharing or transferring electron pairs between atoms. In chemistry and biology they shape molecular structure and function and are generally weaker and more reversible than covalent bonds, enabling dynamic assembly and regulation of complex systems.

Key categories include electrostatic interactions such as ionic bonds and dipole–dipole attractions; hydrogen bonds; and van der Waals forces, including London dispersion and dipole-induced dipole interactions. Other important forms are hydrophobic effects, pi–pi stacking, metal coordination, and cation–π interactions; halogen bonding and chalcogen bonding are increasingly recognized as stabilizing forces in non-covalent assemblies.

Binding strengths typically range from a few to several tens of kilojoules per mole. In solution, solvent molecules compete with the interacting partners, reducing effective strength, but many non-covalent interactions function synergistically and cumulatively provide substantial stabilization.

They play a central role in molecular recognition (such as enzyme–substrate interactions and DNA base pairing), protein folding, and the formation of supramolecular structures. They are essential in drug design, materials science, and catalysis, where selective and reversible binding is advantageous.

Compared with covalent bonds, nietcovalente interactions are reversible and sensitive to temperature, solvent, and ionic strength. They do not create permanent connectivity but confer specificity, adaptability, and the ability to respond to environmental changes.