On the development of proteomics: a brief history.

Although one can trace the roots of proteomics well back into the 20th century, it is basically a discipline of the new millennium. At its outset, it was defined primarily by the technology available to analyze complex mixtures (basically 2D-gel electrophoresis, hybridizations/arrays and mass spectrometry) and what mainly set it aside from protein chemistry, that had flourished since the end of the second world war, was this use of unfractionated starting material as opposed to homogenous samples. Early on, two major new insights were quickly revealed: that the protein complement of cells was overwhelmingly involved in multiple protein–protein interactions and that it was nearly universally involved in a myriad of post-translational modifications. The revelations of the complex networks that result from these two phenomena have created a new understanding of cell biology that has affected our appreciation of such processes as transcription and translation, transmembrane signaling, differentiation, homeostasis and cell death. The development of these methods and strategies that principally characterize the field of proteomics depended heavily on the evolution of those that advanced protein chemistry, particularly during the last half of the twentieth century leading up to the elucidation of the human genome and will be briefly summarized in this article. In the last five decades of the 20th century, the original tools of protein chemistry combined and evolved to form the powerful largely mass spectrometry-based technology known as proteomics. This, together with the burgeoning science of genomics, has allowed the sensitive identification of proteins in complex samples, the principal targets of proteomics, including protein–protein interactions and post-translational modifications and their intricate roles in functional health and disease. [ABSTRACT FROM AUTHOR]