The shape of a protein molecule determines its functionality. Until very recently, a protein’s three-dimensional shape— what chemists call its “secondary structure”— was thought to result from its “primary structure,” the sequence of amino acids that compose it. Current research has challenged this seemingly firm and reasonable assumption. In late-2006, cancer researchers speculated that the timing and pace of protein production can affect its shape without changing its amino acid sequence. This finding indicates an interesting connection between the molecule’s temporal structure (i.e., history) and its shape. We examine the possibility that space-binding and time-binding processes (i.e., molecular structure and bondformation) are closely linked and that learning to manipulate time by influencing timing may be at least as effective as nanotechnological manipulation of the spatial location of individual atoms and molecules.