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  • 1
    ISSN: 1573-5001
    Keywords: FKBP12 ; NMR detection ; sensitivity enhancement ; side chain–side chain hydrogen bonds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We describe the direct observation of side chain–side chain hydrogen bonding interactions in proteins with sensitivity-enhanced NMR spectroscopy. Specifically, the remote correlation between the guanidinium nitrogen 15Nε of arginine 71, which serves as the hydrogen donor, and the acceptor carboxylate carbon 13CO2 γ of aspartate 100 in a 12 kDa protein, human FKBP12, is detected via the trans-hydrogen bond 3h J Nε CO2γ coupling by employing a novel HNCO-type experiment, soft CPD-HNCO. The 3h J Nε CO2γ coupling constant appears to be even smaller than the average value of backbone 3h J NC′ couplings, consistent with more extensive local dynamics in protein side chains. The identification of trans-hydrogen bond J-couplings between protein side chains should provide useful markers for monitoring hydrogen bonding interactions that contribute to the stability of protein folds, to alignments within enzyme active sites and to recognition events at macromolecular interfaces.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5001
    Keywords: FKBP12 ; NMR detection ; sensitivity enhancement ; side chain–main chain hydrogen bonds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We describe the direct observation of very weak side chain–main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins with sensitivity-enhanced NMR spectroscopy. Specifically, the remote correlation between the hydrogen acceptor side chain carboxylate carbon 13CO2 δ of glutamate 54 and the hydrogen donor backbone amide 15N of methionine 49 in a 12 kDa protein, human FKBP12, is detected via the trans-hydrogen bond 3h J NCO2δ coupling by employing a novel sensitivity-enhanced HNCO-type experiment, CPD-HNCO. The 3h J NCO2δ coupling constant appears to be even smaller than the average value of backbone 3h J NC′ couplings, consistent with more extensive local dynamics in protein side chains.
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  • 3
    ISSN: 1573-5001
    Keywords: (H)C(CO)NH-TOCSY ; Multidimensional NMR ; Deuteration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A biosynthetic strategy has recently been developed for the production of 15N, 13C, 2H-labeled proteins using 1H3C-pyruvate as the sole carbon source and D2O as the solvent. The methyl groups of Ala, Val, Leu and Ile (γ2 only) remain highly protonated, while the remaining positions in the molecule are largely deuterated. An (H)C(CO)NH-TOCSY experiment is presented for the sequential assignment of the protonated methyl groups. A high-sensitivity spectrum is recorded on a 15N, 13C, 2H, 1H3C-labeled SH2 domain at 3°C (correlation time 18.8 ns), demonstrating the utility of the method for proteins in the 30–40 kDa molecular weight range.
    Type of Medium: Electronic Resource
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