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  • 13CO/13 $${\text{C}}^\alpha$$ decoupling  (1)
  • 15N chemical shifts  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques (1994)
    Springer
    Journal of biomolecular NMR 4 (1994), S. 845-858 
    Details
    ISSN: 1573-5001
    Keywords: 15N chemical shifts ; Unfolded state ; Pulsed field gradients ; Sensitivity enhanced ; Water suppression ; SH3 domain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter protein, drk, have been assigned. This domain is in slow exchange on the NMR timescale between folded and predominantly unfolded states. Data were collected on both states simultaneously, on samples of the SH3 in near physiological buffer exhibiting an approximately 1:1 ratio of the two states. NMR methods which exploit the chemical shift dispersion of the 15N resonances of unfolded states and pulsed field gradient water suppression approaches for avoiding saturation and dephasing of amide protons which rapidly exchange with solvent were utilized for the assignment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00398413
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  • 2
    Electronic Resource
    Electronic Resource
    Improved lineshape and sensitivity in the HNCO-family of triple resonance experiments (1999)
    Springer
    Journal of biomolecular NMR 14 (1999), S. 273-276 
    Details
    ISSN: 1573-5001
    Keywords: absorptive lineshapes ; 13CO/13 $${\text{C}}^\alpha$$ decoupling ; HNCO ; sensitivity enhancement
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A simple scheme is presented for the suppression of dispersive contributions to cross peaks in HNCO-type spectra where the 15N chemical shift is recorded in a constant-time manner immediately prior to the transfer from 15 N to 1HN at the end of the sequence. These dispersive contributions arise when the delay for refocusing the 15N-13CO one-bond coupling is set to less than 0.5/1JN,CO and when 2 JHN,CO ≠ 0. Improvements in sensitivity in 1HN detected experiments recorded on 15 N,13C-labeled samples can be realized by application of 13CO/13 $${\text{C}}^\alpha$$ decoupling during acquisition. Sensitivity gains on the order of 15% and 5% have been obtained for an SH3 domain (62 residues) and maltose binding protein (370 residues), respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008381929212
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