Proteomics has its roots in analytical biochemical techniques used for protein separation. The first high resolution protein separations were achieved by two-dimensional gel electrophoresis in 1975. Proteomic pioneers such as Leigh Anderson saw the potential of 2-D gels in the late 70s, as a mechanism to conduct proteomic studies of blood proteins and leukocytes. The first computerised 2-D gel image analysis platform was developed to quantitate changes in 2-D gel protein spot levels. While the separation of hundreds of proteins using 2-D gels was welcomed, and changes in protein abundance between samples could be quantitated, frustration also grew with the lack of useful tools to identify proteins of interest. Furthermore, 2-D gel reproducibility hindered the expansion of the technique until the introduction of immobilized pH gradients (IPGs) in 1982, and the much improved second generation IPGs in the late 80s. This coincided with the development of mass spectrometry ionization techniques for peptides, allowing protein identification and characterisation on a large scale. However, it was not until the mid-90s that mass spectrometry became a mainstream technique for protein identification by mostly replacing Edman sequencing.

At the time of Wilkin’s dissertation the genome sequence of Hemophilus influenzae (the first organism to be fully sequenced) was just completed. Over future years with the decoding of additional genomes, the size of translated protein databases ballooned. In today’s proteomic labs it is now possible to robustly separate complex protein mixtures with high resolution, extract the proteins of interest and interrogate them with mass spectrometry, and then ultimately search protein databases using mass spectral data to identify proteins with high confidence. Today’s proteomic practitioners enjoy the legacy of the past 30 years.