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Intramolecular forces such as disulfide bonds give proteins and DNA their structure. Proteins derive their structure from the intramolecular forces that shape them and hold them together. The main source of structure in these molecules is the interaction between the amino acid residues that form the foundation of proteins. [ 7 ]
Many reactions in organic chemistry can occur in either an intramolecular or intermolecular senses. Some reactions are by definition intramolecular or are only practiced intramolecularly, e.g., Dieckmann condensation of diesters is the intramolecular version of aldol condensation. Madelung synthesis of indoles; Smiles rearrangement
Intermolecular forces are weak relative to intramolecular forces – the forces which hold a molecule together. For example, the covalent bond , involving sharing electron pairs between atoms, is much stronger than the forces present between neighboring molecules. [ 1 ]
Strong chemical bonds are the intramolecular forces that hold atoms together in molecules. A strong chemical bond is formed from the transfer or sharing of electrons between atomic centers and relies on the electrostatic attraction between the protons in nuclei and the electrons in the orbitals.
Intramolecular describes a process or phenomenon that occurs within a molecule. It can refer to: Intramolecular reaction; Intramolecular force; See also
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 .
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The most common application of the Hellmann–Feynman theorem is the calculation of intramolecular forces in molecules. This allows for the calculation of equilibrium geometries – the nuclear coordinates where the forces acting upon the nuclei, due to the electrons and other nuclei, vanish.