|Proceedings of the National Academy of Sciences of the United States of America (2004) 101(26):9642-7|
|Northeast Structural Genomics Consortium|
(click to unfold)
A G-matrix Fourier transform (GFT) NMR spectroscopy-based strategy for resonance assignment of proteins is described. ...
Each of the GFT NMR experiments presented here rapidly affords four-, five-, or six-dimensional spectral information in combination with precise measurements of chemical shifts. The resulting high information content enables one to obtain nearly complete assignments by using only four NMR experiments. For the backbone amide proton detected "out-and-back" experiments, data collection was further accelerated up to approximately 2.5-fold by use of longitudinal (1)H relaxation optimization. The GFT NMR experiments were acquired for three proteins with molecular masses ranging from 8.6 to 17 kDa, demonstrating that the proposed strategy is of key interest for automated resonance assignment in structural genomics.
|chemistry methods |
|Molecular Weight Magnetic Resonance Spectroscopy Sensitivity and Specificity Fourier Analysis Bacterial Proteins Peptides |
|107 (Last update: 04/01/2017 12:01:30pm)|
|Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9642-7. Epub 2004 Jun 21.|