October 14, 2002
Volume 80, Number 41
CENEAR 80 41 p. 11
ISSN 0009-2347


NOBEL PRIZE

BIOANALYTICAL TECHNIQUES WIN
Work in mass spec, NMR of proteins leads to chemistry prize

CELIA HENRY

When his wife woke him at 5:30 AM on Oct. 9 with the words "Stockholm's calling," John B. Fenn's first reaction was "Oh my God, can that be?" The answer was yes; he was receiving the 2002 Nobel Prize in Chemistry. "I'm still in a state of shock," he told C&EN that afternoon.

This year's prize recognizes three scientists for developing methods for identification and structure analyses of biological macromolecules. "Many of the recent breakthroughs in drug discovery and design and new treatments for life-threatening diseases are based on the techniques developed by this year's award recipients," notes Nina I. McClelland, chair of the American Chemical Society Board of Directors.

Fenn, 85, emeritus professor at Virginia Commonwealth University, Richmond, shares half the prize with Koichi Tanaka, 43, of the instrument company Shimadzu in Kyoto, Japan, for developing the ionization techniques of electrospray and soft-laser desorption, respectively, for mass spectrometry of proteins. Kurt Wüthrich, 64, professor of molecular biophysics at the Swiss Federal Institute of Technology, Zurich (ETH), and visiting professor at Scripps Research Institute, receives the other half of the $1 million prize for his work on the development of nuclear magnetic resonance techniques to determine the three-dimensional structure of proteins.

Fenn and Tanaka were among the first to extend the powerful technique of mass spectrometry to biological macromolecules. In 1988, Fenn first described his electrospray technique for proteins, in which charged droplets of protein are produced and the solvent is stripped away, leaving only the free protein ions. In 1987, Tanaka demonstrated that laser pulses from a low-energy nitrogen laser could be used to ionize proteins from a surface. These "soft" ionization techniques allow macromolecules to be ionized without fragmenting.

Mass spectrometrists "have been waiting for [a Nobel Prize] in mass spectrometry," says Robert J. Cotter, a mass spectrometrist in the department of pharmacology at Johns Hopkins University School of Medicine. "We're absolutely delighted. Mass spec has been on the rise and is used more and more in biological research everywhere."

Some mass spectrometrists may be disappointed that Franz Hillenkamp of the University of Münster in Germany was not recognized for his development of the technique of matrix-assisted laser desorption ionization (MALDI), the form of soft-laser desorption most often used today.

"It's not being given for MALDI," Cotter says. "It's being given to someone who recognized the path for looking at macromolecules. I personally believe that Tanaka was the first person to see that we could actually go that high."

On the NMR side, Wüthrich has developed a number of methods for determining the three-dimensional structure of proteins. The size of proteins that can be analyzed continues to climb: This summer, Wüthrich reported analyzing the GroEL-GroES complex, which is approximately 900 kilodaltons [Nature, 418, 207 (2002); C&EN, July 15, page 9].

NMR scientists are equally pleased to see Wüthrich receive the prize. "It's great, and it's long overdue that Wüthrich is getting this," says Ad Bax, chief of the biophysical NMR section at the Laboratory of Chemical Physics at NIH. "He's done a fantastic amount of work, starting in the '70s, basically. He's been one of the drivers of this field, and the whole field has flourished because of it."



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