A Faster Way to Determine Protein Structures

A new method for obtaining nuclear magnetic resonance (NMR) data on protein structures is not only much faster than conventional methods but is also less costly and more precise. The method was described in the January 7, 2003, online issue of the Journal of the American Chemical Society.

Called GFT NMR (G-matrix Fourier transform NMR), the method lacks the long measurement times and the low accuracy of frequency measurements common in multidimensional NMR. The G-matrix, which represents a system of linear equations, is used in conjunction with Fourier transform, the mathematical operation used to process multidimensional NMR spectra.

"With GFT NMR, you can record a five- or six-dimensional experiment in about an hour or even less, all because your measurement times increase linearly, not exponentially, with the number of dimensions you are involving,” explained Thomas Szyperski, Ph.D., principal author and associate professor of chemistry and biochemistry at the University of Buffalo (NY, USA; www.buffalo.edu).

Used to determine protein structure since the med-1980s, NMR has been responsible for determining about 20% of the structures in the Protein Data Bank, the international respository of solved protein structures. In comparison, x-ray diffraction has determined about 80%.




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