Molecular Complementarity Permits Tight Highly Specific Binding of Biomolecules

Both inside and outside of cells, ions and molecules are constantly bumping into one another. The greater the number of copies of any two types of molecules per unit volume (i.e., the higher their concentration), the more likely they are to encounter one another. When two molecules encounter each other, they most likely will simply bounce apart because the noncovalent interactions that would bind them together are weak and have a transient existence at physiological temperatures. However, molecules that exhibit molecular complementarity, a lock-and-key kind of fit between their shapes, charges, or other physical properties, can form multiple non-covalent interactions at close range. When two such structurally complementary molecules bump into each other, they can bind (stick) together.

Figure 2-10 illustrates how multiple, different weak bonds can bind two proteins together. Almost any other arrangement of the same groups on the two surfaces would not allow the molecules to bind so tightly. Such multiple, specific interactions between complementary regions within a protein molecule allow it to fold into a unique three-dimensional shape (Chapter 3) and hold the two chains of DNA together in a double helix (Chapter 4). Similar interactions underlie the association of groups of more than two molecules into multi-molecular complexes, leading to formation of muscle fibers, to the gluelike associations between cells in solid tissues, and to numerous other cellular structures.

H N Hydrogen bond


CH3 H3C Hydrophobic

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