Nobel Prizes shared by UK, US and Japanese scientists

The Nobel Prize in Physiology or Medicine for 2002 has been awarded jointly to Sydney Brenner, of Berkeley, California, H. Robert Horvitz, of Cambridge, Massachusetts, and John E. Sulston, of Cambridge in the UK, for their discoveries concerning genetic regulation of organ development and programmed cell death.

By establishing and using the nematode Caenorhabditis elegans as an experimental model system, possibilities were opened to follow cell division and differentiation from the fertilised egg to the adult. The Laureates have identified key genes regulating organ development and programmed cell death and have shown that corresponding genes exist in higher species, including man. The discoveries are important for medical research and have shed new light on the pathogenesis of many diseases.

This year's Nobel Prize in Chemistry was also shared. Half was awarded jointly to John B. Fenn, of Virginia Commonwealth University, Richmond, US, and Koichi Tanaka, of Shimadzu Corp., Kyoto, Japan, for their development of soft desorption ionisation methods for mass spectrometric analyses of biological macromolecules.

The other half of the award went to Kurt Wuethrich, of the Swiss Federal Institute of Technology (ETH), Zuerich, Switzerland and The Scripps Research Institute, La Jolla, US, for his development of nuclear magnetic resonance spectroscopy for determining the three-dimensional structure of biological macromolecules in solution.

Mass spectrometry is an analytical method used in chemistry laboratories the world over. Previously only fairly small molecules could be identified, but Fenn and Tanaka have developed methods that make it possible to analyse biological macromolecules as well.

Wuethrich has made it possible to use nuclear magnetic resonance (NMR) on proteins. He developed a general method of systematically assigning certain fixed points in the protein molecule, and also a principle for determining the distances between these. Using the distances, he was able to calculate the three-dimensional structure of the protein. The advantage of NMR is that proteins can be studied in solution, i.e. an environment similar to that in the living cell.