9 October 2002
The Royal Swedish Academy of Sciences has decided to
award the Nobel Prize in Chemistry for 2002
”for the development of methods for identification and structure analyses of biological macromolecules”
with one half jointly to
John B. Fenn
Virginia Commonwealth University, Richmond, USA, and
Shimadzu Corp., Kyoto, Japan
”for their development of soft
desorption ionisation methods for mass spectrometric analyses of
and the other half to
Swiss Federal Institute of Technology (ETH), Zürich, Switzerland and The Scripps Research Institute, La Jolla, USA
”for his development of nuclear magnetic resonance spectroscopy for determining the three-dimensional structure of biological macromolecules in solution”.
This year’s Nobel Prize in Chemistry
concerns powerful analytical methods for studying biological
macromolecules, for example proteins. The possibility of
analysing proteins in detail has led to increased understanding
of the processes of life. Researchers can now rapidly and simply
reveal what different proteins a sample contains. They can also
determine three-dimensional pictures showing what protein
molecules look like in solution and can then understand their
function in the cell. The methods have revolutionised the
development of new pharmaceuticals. Promising applications are
also being reported in other areas, for example foodstuff control
and early diagnosis of breast cancer and prostate cancer.
Mass spectrometry is a very important analytical method used in practically all chemistry laboratories the world over. Previously only fairly small molecules could be identified, but John B. Fenn and Koichi Tanaka have developed methods that make it possible to analyse biological macromolecules as well.
In the method that John B. Fenn published in 1988, electrospray ionisation (ESI), charged droplets of protein solution are produced which shrink as the water evaporates. Eventually freely hovering protein ions remain. Their masses may be determined by setting them in motion and measuring their time of flight over a known distance. At the same time Koichi Tanaka introduced a different technique for causing the proteins to hover freely, soft laser desorption. A laserpulse hits the sample, which is “blasted” into small bits so that the molecules are released.
The other half of the Prize rewards the further development of another favourite method among chemists, nuclear magnetic resonance, NMR. NMR gives information on the three-dimensional structure and dynamics of the molecules. Through his work at the beginning of the 1980s Kurt Wüthrich has made it possible to use 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.
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John B. Fenn, born 1917 (85 years)
in New York City, USA (US citizen). PhD in Chemistry 1940 and
Professor Emeritus 1987 at Yale University, Connecticut, USA.
Since 1994 Research Professor at Virginia Commonwealth
University, Richmond, Virginia, USA.
Koichi Tanaka, born 1959 (43 years)
in Toyama City, Japan (Japanese citizen). B. Eng at Tohoku
University, Japan. R&D Engineer at Shimadzu Corp., Kyoto,
Kurt Wüthrich, born 1938 (64
years) in Aarberg, Switzerland (Swiss citizen). PhD in Inorganic
chemistry 1964 at the University of Basel, Switzerland. Professor
in Biophysics at ETH Zürich, Switzerland and Visiting
Professor at the Scripps Research Institute, La Jolla,
Prize amount: SEK 10 million. Fenn and Tanaka share one half and Wüthrich receives the other half
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