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  • high molecular weight proteins  (2)
  • 13CO/13 $${\text{C}}^\alpha$$ decoupling  (1)
  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    A 4D TROSY-based pulse scheme for correlating 1HNi,15Ni,13Cαi,13C′i−1 chemical shifts in high molecular weight, 15N,13C, 2H labeled proteins (1999)
    Springer
    Journal of biomolecular NMR 15 (1999), S. 309-313 
    Details
    ISSN: 1573-5001
    Keywords: 4D NMR ; deuteration ; high molecular weight proteins ; protein assignment ; triple resonance NMR ; TROSY
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A 4D TROSY-based triple resonance experiment, 4D-HNCOi−1CAi, is presented which correlates intra-residue 1HN, 15N, 13 Cα chemical shifts with the carbonyl (13C′) shift of the preceding residue. The experiment is best used in concert with recently described 4D TROSY-HNCOCA and -HNCACO experiments [Yang, D. and Kay, L.E. (1999) J. Am. Chem. Soc., 121, 2571–2575]. In cases where degeneracy of (1HN,15N) spin pairs precludes assignment using the HNCOCA and HNCACO, the HNCOi−1CAi often allows resolution of the ambiguity by linking the 13Cα and 13C′ spins surrounding the (1HN,15N) pair. The experiment is demonstrated on a sample of 15N, 13C, 2 H labeled maltose binding protein in complex with β-cyclodextrin that tumbles with a correlation time of 46 ns.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008310617047
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  • 3
    Electronic Resource
    Electronic Resource
    A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment (2000)
    Springer
    Journal of biomolecular NMR 18 (2000), S. 183-188 
    Details
    ISSN: 1573-5001
    Keywords: deuteration ; high molecular weight proteins ; methyl protonation ; residual dipolar couplings
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A method for incorporating dipolar coupling restraints into structure calculations is described which follows closely on methodology that has been recently presented for orienting peptide planes using dipolar couplings [Mueller et al. (2000) J. Mol. Biol., 300, 197–212] and is specifically developed for use in cases of an axially symmetric alignment tensor. Modeling studies on an all α-helical protein, farnesyl diphosphate synthase, establish the utility of the approach. A global fold of the 370-residue maltose binding protein in complex with β-cyclodextrin is obtained from experimentally derived restraints. The average pairwise rmsd values between the N- and C-terminal domains in this NMR structure and the corresponding regions in the X-ray structure of the protein are 2.8 and 3.1 Å, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026788430236
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