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Noncovalent Bonding

Noncovalent bonding

There are three principle kinds of noncovalent forces.

1. Ionic Interactions

At any given pH, proteins have charged groups that may participate in binding them to each other or to other types of molecules. For example, as the figure shows, negatively-charged carboxyl groups on aspartic acid (Asp) and glutamic acid (Glu) residues may be attracted by the positively-charged free amino groups on lysine (Lys) and arginine (Arg) residues.

Ionic interactions are highly sensitive to

2. Hydrophobic Interactions

The side chains (R groups) of such amino acids as phenylalanine and leucine are nonpolar and hence interact poorly with polar molecules like water. For this reason, most of the nonpolar residues in globular proteins are directed toward the interior of the molecule whereas such polar groups as aspartic acid and lysine are on the surface exposed to the solvent. When nonpolar residues are exposed at the surface of two different molecules, it is energetically more favorable for their two "oily" nonpolar surfaces to approach each other closely displacing the polar water molecules from between them.

The strength of hydrophobic interactions is not appreciably affected by changes in pH or in salt concentration.

3. Hydrogen Bonds

Hydrogen bonds can form whenever

Some common examples:

Link to a separate page on hydrogen bonds.

Noncovalent interactions are individually weak but collectively strong.

All three forms of noncovalent interactions are individually weak (on the order of 5 kcal/mole) as compared with a covalent bond (with its 90–100 kcal/mole of bond energy). And what strength these interactions do have requires that the interacting groups can approach each other closely (an angstrom or less). So we can conclude that all the examples given at the top of the page require:


24 February 2011