- hydrogen bonding
Interaction involving a hydrogen atom located between a pair of other atoms having a high affinity for electrons; such a bond is weaker than an ionic bond or covalent bond but stronger than van der Waals forces.Hydrogen bonds can exist between atoms in different molecules or in parts of the same molecule. One atom of the pair (the donor), generally a fluorine, nitrogen, or oxygen atom, is covalently bonded to a hydrogen atom (―FH, ―NH, or ―OH), whose electrons it shares unequally; its high electron affinity causes the hydrogen to take on a slight positive charge. The other atom of the pair, also typically F, N, or O, has an unshared electron pair, which gives it a slight negative charge. Mainly through electrostatic attraction, the donor atom effectively shares its hydrogen with the acceptor atom, forming a bond. Because of its extensive hydrogen bonding, water (H2O) is liquid over a far greater range of temperatures that would be expected for a molecule of its size. Water is also a good solvent for ionic compounds and many others because it readily forms hydrogen bonds with the solute. Hydrogen bonding between amino acids in a linear protein molecule determines the way it folds up into its functional configuration. Hydrogen bonds between nitrogenous bases in nucleotides on the two strands of DNA (guanine pairs with cytosine, adenine with thymine) give rise to the double-helix structure that is crucial to the transmission of genetic information.
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