Measuring macromolecular diffusion using heteronuclear multiple-quantum pulsed-field-gradient NMR. Dingley, A., Mackay, J., Shaw, G., Hambly, B., & King, G. Journal of Biomolecular NMR, 10(1):1-8, 1997. doi abstract bibtex 1 download We have previously shown that 1H pulsed-field-gradient (PFG) NMR spectroscopy provides a facile method for monitoring protein self-association and can be used, albeit with some caveats, to measure the apparent molecular mass of the diffusant [Dingley et al. (1995) J. Biomol. NMR, 6, 321-328]. In this paper we show that, for 15N-labelled proteins, selection of 1H-15N multiple-quantum (MQ) coherences in PFG diffusion experiments provides several advantages over monitoring 1H single-quantum (SQ) magnetization. First, the use of a gradient-selected MQ filter provides a convenient means of suppressing resonances from both the solvent and unlabelled solutes. Second, 1H-15N zero-quantum coherence dephases more rapidly than 1H SQ coherence under the influence of a PFG This allows the diffusion coefficients of larger proteins to be measured more readily. Alternatively, the gradient length and/or the diffusion delay may be decreased, thereby reducing signal losses from relaxation. In order to extend the size of macromolecules to which these experiments can be applied, we have developed a new MQ PFG diffusion experiment in which the magnetization is stored as longitudinal two-spin order for most of the diffusion period, thus minimizing sensitivity losses due to transverse relaxation and J-coupling evolution.
@article{
title = {Measuring macromolecular diffusion using heteronuclear multiple-quantum pulsed-field-gradient NMR},
type = {article},
year = {1997},
pages = {1-8},
volume = {10},
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abstract = {We have previously shown that 1H pulsed-field-gradient (PFG) NMR spectroscopy provides a facile method for monitoring protein self-association and can be used, albeit with some caveats, to measure the apparent molecular mass of the diffusant [Dingley et al. (1995) J. Biomol. NMR, 6, 321-328]. In this paper we show that, for 15N-labelled proteins, selection of 1H-15N multiple-quantum (MQ) coherences in PFG diffusion experiments provides several advantages over monitoring 1H single-quantum (SQ) magnetization. First, the use of a gradient-selected MQ filter provides a convenient means of suppressing resonances from both the solvent and unlabelled solutes. Second, 1H-15N zero-quantum coherence dephases more rapidly than 1H SQ coherence under the influence of a PFG This allows the diffusion coefficients of larger proteins to be measured more readily. Alternatively, the gradient length and/or the diffusion delay may be decreased, thereby reducing signal losses from relaxation. In order to extend the size of macromolecules to which these experiments can be applied, we have developed a new MQ PFG diffusion experiment in which the magnetization is stored as longitudinal two-spin order for most of the diffusion period, thus minimizing sensitivity losses due to transverse relaxation and J-coupling evolution.},
bibtype = {article},
author = {Dingley, A.J. and Mackay, J.P. and Shaw, G.L. and Hambly, B.D. and King, G.F.},
doi = {10.1023/A:1018339526108},
journal = {Journal of Biomolecular NMR},
number = {1}
}
Downloads: 1
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