Frederick Sanger (1918–2013)

The scientific community recently lost one of its brightest, imaginative, and humble scientists with the quiet passing of Fred Sanger, at age 95. He is well known for his pioneering work inventing key methods for both protein and nucleic acid sequencing, studies that resulted in his winning two Nobel prizes in chemistry.

Fred’s scientific career began as a student at St. John’s College, Cambridge University, UK, studying amino acids and their metabolism. While there, he developed methods for protein sequencing that included the “Sanger reagent” and the concept that short, sequenced peptides could be assembled based on their sequence overlap to build large polypeptides. Those studies resulted in completing the primary structure of several proteins, including insulin, which led to his first Nobel Prize in Chemistry in 1958. These groundbreaking studies served as the foundation for our understanding of protein structure and function, and the rules that form the basis of our knowledge of enzymology, as well as nonenzymatic structural proteins. His work also set the stage for developing the concept that the primary protein chain becomes folded to form a three-dimensional protein that can be stabilized by amino acid interactions, whether hydrophobic, hydrophilic, or disulfide bonds. His new and innovative protein structural methods then were extended by others and resulted in automated protein sequencing with instruments that could accomplish in a few days what had previously taken several years of bench work.

In 1962, Fred moved to the newly formed Medical Research Council’s Laboratory of Molecular Biology (MRC-LMB), where the faculty at the MRC-LMB had a deep interest in molecular biology. Even though he was the head of the protein chemistry division, his thoughts turned to nucleic acids and he began developing new methods for sequencing RNA. These studies then evolved …