The forces, either attractive or repulsive, that exist between molecules due to electric charges or varying electron cloud distribution. This tag could also include intra-molecular attractions (within one molecule itself) often found in a protein amino acid residues.
The forces, either attractive or repulsive, that exist between molecules due to electric charges or varying electron cloud distribution. The major types of inter-molecular forces are:
- Dipole-dipole
- Ion-dipole
- Hydrogen bonding
- Van der Waals forces
- London Dispersion (a type of VdW) between non-polar molecules
The other types are intra-molecular interactions/forces which are often found within a protein amino acid residues. Such as,
- non-covalent ionic interactions (part of a salt bridge)
- salt bridges
Salt bridge is formed with a combination of two non-covalent interactions namely a hydrogen bond and an ionic interaction (coulombic) between two oppositely charged residues (with full-electron charges) that are sufficiently close to each other to experience electrostatic interaction. Salt bridges are elementary motifs of protein secondary and tertiary structure and are commonly associated with structural driving force that increases stability. Often found on the interface to the solvent, they are highly susceptible to solvent–solute interactions, primarily with water but also with other cosolvents (especially ions).
