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  • 1
    Electronic Resource
    Electronic Resource
    Measurement of the protein backbone dihedral angle φ based on quantification of remote CSA/DD interference in inter-residue 13C′(i − 1)-13Cα(i) multiple-quantum coherences (2000)
    Springer
    Journal of biomolecular NMR 17 (2000), S. 265-268 
    Details
    ISSN: 1573-5001
    Keywords: chemical shift anisotropy ; cross-correlated spin relaxation ; dihedral angles ; multiple-quantum coherence ; structure determination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A novel triple-resonance NMR method is presented for the measurement of the protein backbone dihedral angle φ based on differential multiple-quantum relaxation induced by relaxation interference between 1Hα(i)-13Cα(i) dipolar and 13C′(i−1) (carbonyl) chemical shift anisotropy mechanisms. The method employs a simultaneous transfer of 15N magnetization to the inter- and intra-residue 13Cα carbons as well as the directly attached carbonyl carbon 13C′. Results obtained on 13C,15N-labeled ubiquitin demonstrate the potential of the method.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008393903160
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  • 2
    Electronic Resource
    Electronic Resource
    Heteronuclear relaxation in time-dependent spin systems: 15N-T1ρ dispersion during adiabatic fast passage (1999)
    Springer
    Journal of biomolecular NMR 13 (1999), S. 213-221 
    Details
    ISSN: 1573-5001
    Keywords: adiabatic fast passage ; 15N NMR ; heteronuclear relaxation ; protein dynamics ; T1ρ-dispersion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A novel NMR experiment comprising adiabatic fast passage techniques for the measurement of heteronuclear self-relaxation rates in fully 15N-enriched proteins is described. Heteronuclear self-relaxation is monitored by performing adiabatic fast passage (AFP) experiments at variable adiabaticity (e.g., variation of RF spin-lock field intensity). The experiment encompasses gradient- selection and sensitivity-enhancement. It is shown that transverse relaxation rates derived with this method are in good agreement with the ones measured by the classical Carr–Purcell–Meiboom–Gill (CPMG) sequences. An application of this method to the study of the carboxyl-terminal LIM domain of quail cysteine and glycine-rich protein qCRP2(LIM2) is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008324721356
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