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  • 1
    ISSN: 1573-5001
    Keywords: Pulsed-field-gradient NMR ; Translational diffusion coefficient ; Self-association ; Macromolecules ; Solvent suppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have previously shown that 1H pulsed-field-gradient(PFG) NMR spectroscopy provides a facile method for monitoring proteinself-association and can be used, albeit with some caveats, to measure theapparent molecular mass of the diffusant [Dingley et al. (1995) J. Biomol.NMR, 6, 321–328]. In this paper we show that, for15N-labelled proteins, selection of1H-15N multiple-quantum (MQ) coherences in PFGdiffusion experiments provides several advantages over monitoring1H single-quantum (SQ) magnetization. First, the use of agradient-selected MQ filter provides a convenient means of suppressingresonances from both the solvent and unlabelled solutes. Second,1H-15N zero-quantum coherence dephases morerapidly than 1H SQ coherence under the influence of a PFG.This allows the diffusion coefficients of larger proteins to be measuredmore readily. Alternatively, the gradient length and/or the diffusion delaymay be decreased, thereby reducing signal losses from relaxation. In orderto extend the size of macromolecules to which these experiments can beapplied, we have developed a new MQ PFG diffusion experiment in which themagnetization is stored as longitudinal two-spin order for most of thediffusion period, thus minimizing sensitivity losses due to transverserelaxation and J-coupling evolution.
    Type of Medium: Electronic Resource
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