Synge, Richard Laurence Millington (1914–1994)

British biochemist who improved paper chromatography (a means of separating mixtures) to the point where individual amino acids could be identified. He shared the Nobel Prize for Chemistry in 1952 with his colleague Archer Martin for the development in 1944 of the technique known as partition chromatography.

Martin and Synge worked together at Cambridge and at the Wool Industries Research Association in Leeds, Yorkshire. Their chromatographic method became an immediate success, widely adopted. It was soon demonstrated that not only the type but the concentration of each amino acid can be determined.

Life Synge was born in Liverpool and studied at Winchester College and at Cambridge University. In 1948 he moved to the Rowett Research Institute, Aberdeen, Scotland, where he remained in charge of protein chemistry until 1967. From 1967 until his retirement in 1974 he worked as a biochemist at the Food Research Institute of the Agricultural Research Council in Norwich. He was also honorary professor of biology at the University of East Anglia. Synge was very active in the peace movement.

Paper chromatography In the early 1940s there were only crude chromatographic techniques available for separating proteins in reasonably large samples; no method existed for the separation of the amino acids that make up proteins. Martin and Synge developed the technique of paper chromatography, using porous filter paper to separate out amino acids using a solvent. A minute quantity of the amino acid solution is placed near the edge of the filter paper; once dry, it is dipped (or suspended) in a solvent. As the solvent passes the mixture, the amino acids move with it, but they do so at different rates and so become separated. Once dry, the paper is sprayed with a developer and the amino acids show up as coloured dots. Synge and Martin announced their technique in 1944; it was soon being applied to a wide variety of experimental problems.

Paper chromatography is so precise that it can be used to identify amino acid concentration, as well as type, enabling Synge to work out the exact structure of the antibiotic peptide Gramicidin-S, a piece of research important to Frederick Sanger's determination of the structure of insulin in 1953.