The Dreyer Peptide and Protein Sequencer

Credit: Courtesy of Alan Hawk / Historical Collections National Museum of Health and Medicine" /> Credit: Courtesy of Alan Hawk / Historical Collections National Museum of Health and Medicine As biochemists during the 1970s delved into the protein chemistry of cell signaling, cycling, and adhesion, they ran into two major obstacles: getting enough purified material for some proteins, and the low molecular weights of others. Interferon, for example, was so difficult to purify that it

Terry Sharrer
Jul 1, 2007
<figcaption> Credit: Courtesy of Alan Hawk / Historical Collections National Museum of Health and Medicine</figcaption>
Credit: Courtesy of Alan Hawk / Historical Collections National Museum of Health and Medicine

As biochemists during the 1970s delved into the protein chemistry of cell signaling, cycling, and adhesion, they ran into two major obstacles: getting enough purified material for some proteins, and the low molecular weights of others. Interferon, for example, was so difficult to purify that it took more than two decades before its structural characterization. And tiny proteins like angiotensin II (8 amino acids) and the antidiuretic hormone vasopressin (9 amino acids) produced hard-to-interpret protein signatures.

Biochemists were constantly pushing the limits of technology to couple, cleave, extract, and sequence peptides with better sensitivity. Pehr Edman, in 1950, developed a chemical degradation process for amino acid sequencing and built the first automated "sequenator" for that task in 1967. Richard Laursen, at Boston University, improved on Edman's concept in 1971 by immobilizing the study sample on a...

References

1. W.J. Dreyer, "Peptide or protein sequencing method and apparatus," US patent No. 4,065,412, issued Dec. 27, 1977. 2. Interview with William J. Dreyer, Oral History Project, California Institute of Technology Archives, 2005. http://oralhistories.library.caltech.edu/108/01/OH_Dreyer_W.pdf