Richard Laurence Millington Synge




ENGLISH BIOCHEMIST
1914–1994

Richard Laurence Millington Synge's fascination with biochemistry came into being when he was a young man. In his 1952 Nobel Lecture, he revealed that, at the age of nineteen, after reading Sir Frederick Hopkins's presidential address to the British Association for the Advancement of Science, he suddenly realized "that living things must have wonderfully precise and complicated working parts on the molecular scale, and that biochemists had the best chance of finding out how these are put together and do their work" (Synge, "Applications of Partition Chromatograpy"). It was his desire to unravel the complicated molecules of biochemical importance that ultimately led to his collaboration with Archer J. P. Martin and to their development of liquid-liquid partition chromatography .

Having completed his undergraduate training in biochemistry and having acquired a familiarity with biochemical techniques, Synge launched into a chemical study of glycoproteins. A short time later he changed course: "Soon I found that my knowledge both of carbohydrate and protein chemistry was inadequate to the task" (Synge, "Applications of Partition Chromatography"). Synge moved on to work with Dr. D. J. Bell, under whose

British chemist Richard Laurence Millington Synge, co-recipient, with Archer John Porter Martin, of the 1952 Nobel Prize in chemistry, "for their invention of partition chromatography."
British chemist Richard Laurence Millington Synge, co-recipient, with Archer John Porter Martin, of the 1952 Nobel Prize in chemistry, "for their invention of partition chromatography."

instruction he came to appreciate the power of liquid-liquid extraction as a method of separating the components of chemical mixtures.

It was as a graduate student at Cambridge University that Synge came into contact with Dr. Hedley R. Marston, who advised Synge to study the amino acid composition of wool. The acetylamino acids that were generated during the course of Synge's analysis of wool proteins were partitionable between chloroform and water. Synge was encouraged to consult with Martin on how best to achieve this partitioning.

The collaboration between Martin and Synge eventually culminated in a demonstration of partition chromatography to the Biochemical Society at its meeting at the National Institute for Medical Research in London, on June 7, 1941, followed by the publication of their results in Biochemical Journal (1941).

Although Synge did not pursue the further development of chromatographic methods with Martin, he did employ techniques that had been developed by Martin to investigate large peptides. From 1942 to 1948 Synge worked almost exclusively with antibiotic peptides of the gramicidin group, employing paper chromatography to elucidate their primary structures (amino acid sequences). Breaking up these peptides into dipeptide and tripeptide fragments, Synge recognized that identification of these fragments led back to the original sequences. That is, an A–B–C–D–E chain will give rise to the fragments A–B, B–C, C–D, and D–E, from which the original sequence can be unequivocally reconstructed.

SEE ALSO Glycoprotein ; Martin, Archer John Porter ; Primary Structure .

Todd W. Whitcombe

Bibliography

Martin, A. J. P.; Synge, Richard Laurence Millington (1941). Biochemical Journal 35: 1,358–1,366.

Shetty, Prabhakara H. (1993). "Richard Laurence Millington Synge." In Nobel Laureates in Chemistry 1901–1992, ed. Laylin K. James. Washington, DC: American Chemical Society; Chemical Heritage Foundation.

Internet Resources

"Richard Laurence Millington Synge—Biography." Nobel e-Museum. Available from http://www.nobel.se .

Synge, Richard Laurence Millington (1952). "Applications of Partition Chromatography," Nobel Lecture, December 12, 1952. Available from http://www.nobel.se/chemistry/laureates/1952/synge-lecture.html .



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