G-matrix Fourier transform (GFT) NMR, a technique developed several years ago for rapid collection of nuclear magnetic resonance data, has been used to determine the structures of eight proteins in less than a month.1 "People usually work for many months for one structure. And even a year is not unusual," says coauthor Thomas Szyperski of the University of Buffalo. [see related story, page 36]
The work demonstrates for the first time that GFT NMR works on a "real world" scale, meaning a protein concentration of 1 mM and proteins up to 22 kD in size, says biophysical chemist Xiaolian Gao of the University of Houston.
High-dimensional NMR experiments require sampling from indirect dimensions, which increases instrument run times. In GFT NMR, however, several indirect dimensions are sampled simultaneously, dramatically speeding up resonance assignment data acquisition. To make the process more high-throughput, the researchers combined it with simultaneous heteronuclear NOESY...
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