Szyperski Shares Major NMR Prize

BUFFALO, N.Y. -- Thomas Szyperski, Ph.D., University at Buffalo professor of chemistry, biochemistry and structural biology, is a co-recipient of one of the most prestigious prizes awarded in the field of nuclear magnetic resonance spectroscopy, the Günther Laukien Prize.

The prize was awarded April 24 at the 47th Experimental Nuclear Magnetic Resonance Conference in Pacific Grove, Calif.

The Laukien Prize was established in 1999 in memory of Günther Laukein, a co-founder of Bruker BioSpin, a leading supplier of NMR spectrometers.

It carries a monetary award of $15,000 funded by Bruker BioSpin and is intended "to recognize cutting-edge experimental NMR research with a high probability of enabling beneficial new applications."

This year, the award will be shared equally between Szyperski; Rafael Bruschweiler, professor of chemistry and biochemistry at Florida State University, and the team of Eriks Kupce, principal scientist at Varian Ltd., and Ray Freeman of Cambridge University.

Szyperski is being recognized for his seminal contributions to the design of rapid acquisition techniques of multidimensional NMR spectra.

A team of UB structural genomics scientists led by him received major international attention in 2003 when it published a new method of using NMR (called GFT-NMR), a much faster, more precise and far-less-expensive method of obtaining nuclear magnetic resonance data to map a protein's atomic structure.

For that development, he was named one of Scientific American's Top 50 contributors to science and technology in 2003.

Last summer, Szyperski and his team published a paper on how they used the method to determine the structures of eight proteins in just 10-20 days per protein, a process that typically takes an average of six to 12 months to solve a single protein using conventional NMR methods.

The patented method was able to solve membrane proteins, considered by some to be the "holy grail" of structural genomics and highly prized in rational drug design.

Now the method has been widely adopted throughout the genomics community as one of the best ways to use NMR for protein-structure determination.

Szyperski and his team are expected to use the new method to solve between 12 and 15 structures per year for the National Institutes of Health-funded Northeast Structural Genomics Consortium (NESG), part of the Protein Structure Initiative.

Their success to date has attracted approximately $4 million in new federal research funds to Szyperski's lab over the next five years from the Protein Structure Initiative; the New York Center on Membrane Protein Structure, an NIH-funded center of the PSI, and the Molecular and Cellular Biophysics Division of the National Science Foundation.

Szyperski, a UB faculty member since 1998, is director of the university's high-field NMR facility and an adjunct senior researcher at the Hauptman-Woodward Medical Research Institute.

He also is a recipient of the American Chemical Society's Buck-Whitney Medal.

Szyperski lives in Amherst.