@article{
 title = {Measuring macromolecular diffusion using heteronuclear multiple-quantum pulsed-field-gradient NMR},
 type = {article},
 year = {1997},
 pages = {1-8},
 volume = {10},
 id = {53beac46-6091-3dfa-988a-801d2a1ac05f},
 created = {2023-01-10T01:46:52.607Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:46:52.607Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 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}
}

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(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. 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