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Non-covalent interactions can be classified into different categories, such as electrostatic, π-effects, van der Waals forces, and hydrophobic effects. [3] [2] Non-covalent interactions [4] are critical in maintaining the three-dimensional structure of large molecules, such as proteins and nucleic acids.
In supramolecular chemistry, [1] host–guest chemistry describes complexes that are composed of two or more molecules or ions that are held together in unique structural relationships by forces other than those of full covalent bonds. Host–guest chemistry encompasses the idea of molecular recognition and interactions through non-covalent ...
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 ]
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]
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 ...
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]
Supramolecular polymers are a subset of polymers where the monomeric units are connected by reversible and highly directional secondary interactions–that is, non-covalent bonds. These non-covalent interactions include van der Waals interactions, hydrogen bonding, Coulomb or ionic interactions, π-π stacking, metal coordination, halogen ...
In biochemistry, a protein dimer is a macromolecular complex or multimer formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word dimer has roots meaning "two parts", di-+ -mer. A protein dimer is a type of protein quaternary structure.