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  • 1
    Electronic Resource
    Electronic Resource
    NMR detection of side chain–side chain hydrogen bonding interactions in 13C/15N-labeled proteins (2000)
    Springer
    Journal of biomolecular NMR 17 (2000), S. 305-310 
    Details
    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
    URL: http://dx.doi.org/10.1023/A:1008390813387
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  • 2
    Electronic Resource
    Electronic Resource
    Detection of very weak side chain–main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy (2000)
    Springer
    Journal of biomolecular NMR 17 (2000), S. 79-82 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008373501591
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Solution structure of actinomycin-DNA complexes: Drug intercalation at isolated G-C sites (1991)
    Springer
    Journal of biomolecular NMR 1 (1991), S. 323-347 
    Details
    ISSN: 1573-5001
    Keywords: Drug-DNA interaction ; Actinomycin ; Restrained molecular dynamics ; Nuclear Overhauser effect ; NOE ; 2D NMR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The actinomycin-D-d(A1-A2-A3-G4-C5-T6-T7-T8) complex (1 drug per duplex) has been generated in aqueous solution and its structure characterized by a combined application of two-dimensional NMR experiments and molecular dynamics calculations. We have assigned the exchangeable and nonexchangeable proton resonances of Act and d(A3GCT3) in the complex and identified the intermolecular proton-proton NOES that define the alignment of the antitumor agent at its binding site on duplex DNA. The molecular dynamics calculations were guided by 70 intermolecular distance constraints between Act and nucleic acid protons in the complex. The phenoxazone chromophore of Act intercalates at the (G-C)I·(G-C)II step in the d(A3GCT3) duplex with the phenoxazone ring stacking selectively with the G4I and G4II purine bases but not with C4I and C4II pyrimidine bases at the intercalation site. There is a pronounced unwinding between the A3·T6 and G4·C5 base pairs which are the next steps located in either direction from the intercalation site in the Act-d(A3GCT3) complex. The Act cyclic pentapeptide ring conformations in the complex are similar to those for free Act in the crystal except for a change in orientation of the ester linkage connecting meVal and Thr residues. The cyclic pentapeptide rings are positioned in the minor groove with the established G-C sequence specificity of binding associated with intermolecular hydrogen bonds between the Thr backbone CO and NH groups to the NH2-2 and N3 positions of guanosine, respectively. Complex formation is also stabilized by van der Waals interactions between nonpolar groups on the cyclic pentapeptide rings and the sugar residues and base pair edges lining the widened minor groove of the (A3-G4-C5-T6)I·(A3-G4-C5-T6)II binding site segment of the DNA helix.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02192858
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    Paper (German National Licenses)
    Fulltext
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