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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 ]
Intramolecular nonbonded interactions are counted only for atoms three or more bonds apart; 1,4 interactions are scaled down by the "fudge factor" =, otherwise =. All the interaction sites are centered on the atoms; there are no "lone pairs".
Intramolecular reactions, especially ones leading to the formation of 5- and 6-membered rings, are rapid compared to an analogous intermolecular process. This is largely a consequence of the reduced entropic cost for reaching the transition state of ring formation and the absence of significant strain associated with formation of rings of these ...
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.
It is usually manifested in intermolecular reactions, whereas discussion of steric effects often focus on intramolecular interactions. Steric hindrance is often exploited to control selectivity, such as slowing unwanted side-reactions. Steric hindrance between adjacent groups can also affect torsional bond angles.
In molecular physics and chemistry, the van der Waals force (sometimes van de Waals' force) is a distance-dependent interaction between atoms or molecules. Unlike ionic or covalent bonds , these attractions do not result from a chemical electronic bond ; [ 2 ] they are comparatively weak and therefore more susceptible to disturbance.
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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 .