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The finding may explain how RNA sequences define the final, folded form of a protein—a fundamental problem in molecular biology, since proteins need to fold in order to function.

The Japanese scientist Susumu Tonegawa received the 1987 Nobel Prize in Physiology or Medicine for revealing the clever way in which a relatively small number of genes could create so many possible antibodies. Working in the Basel Institute of Immunology in the 1970s (which at the time was headed by Nils Jerne), he found that individual antibodies are assembled on a biological ‘production line’ from several genes. Each gene that encodes the heavy and light protein chain components are unlike regular, single genes; they are instead made up of many units, like a string of pearls. To create an antibody, one unit or 'pearl' from each component gene is selected randomly and stuck together to form the finished product. As a result of this selection and assembly process, millions of possible combinations can be produced.