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  • 1
    Electronic Resource
    Electronic Resource
    A Combined Molecular Modelling and CIDNP Study of Similarities in the Pattern of Ligand Binding in Mammalian and Avian Galectins (1997)
    Springer
    Journal of molecular modeling 3 (1997), S. 325-331 
    Details
    ISSN: 0948-5023
    Keywords: Keywords: Surface accessibility ; Molecular Dynamics ; Homology modelling ; Carbohydrate binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Galectins (Galactose binding lectins) from bacteria, plants and animals have been shown to possess tyrosine or tryptophan residues that form hydrophobic contacts with their ligands in the binding sites. At the present time, the X-ray structures of only two galectins from human and bovine tissues are known. In the present study we applied X-ray data of bovine heart galectin-1 as a template for homology modelling of a number of galectins from mammalian and avian tissues. The conservation of one tryptophan and at least one histidine in binding pocket can be observed from the comparison of the model structures. We also show that it is possible to obtain information of the architecture of the binding pocket of several galectins in solution using CIDNP (Chemically Induced Dynamic Nuclear Polarisation) techniques. The CIDNP approach offers a possibility to analyse these lectins in solution thereby providing supplementary information to the available X-ray data. All studied galectins show comparable alterations when they are recorded by CIDNP-technique in the absence and in the presence of their specific carbohydrate ligands.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s008940050046
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  • 2
    Electronic Resource
    Electronic Resource
    Comparison between intact and desialylated human serum amyloid P component by laser photo CIDNP (chemically induced dynamic nuclear polarization) technique: an indication for a conformational impact of sialic acid (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 945-949 
    Details
    ISSN: 1573-4986
    Keywords: human serum amyloid P component (SAP) ; chemically induced dynamic nuclear polarization (CIDNP) ; glycoprotein ; sialic acid ; protein conformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The human pentraxin serum amyloid P component (SAP) exhibits no microheterogeneity in its complex di-antennary glycan. To elucidate whether the removal of sialic acids from this glycoprotein might affect the accessibility of certain amino acid residues of the protein we employed the laser photo CIDNP approach as a sensitive tool. The CIDNP effect is generated by the interaction of a photoexcited dye with reactive amino acids and results in enhanced absorption- or emission-signals which can be observed for the three aromatic amino acids histidine, tryptophan, and tyrosine if they are accessible to the dye. Therefore, this technique can be applied to explore surface exposure of these amino acid residues. The respective spectra of SAP and enzymatically desialylated SAP were determined. Six tryptophan/histidine signals and one tyrosine signal are present in the aromatic part of the CIDNP difference spectrum of SAP. The corresponding spectrum of desialylated SAP shows remarkable alterations. The chemical shift of one Trp/His-characteristic signal is decreased by 0.1 ppm. One Trp/His-signal disappeared and a new one was formed in the CIDNP difference spectrum of desialylated SAP, while the other signals were unaffected. The Tyr signal has a clearly enhanced intensity in desialylated SAP. Therefore, the removal of sialic acid moieties from the single N-glycan of each monomer apparently affects surface presentation of distinct CIDNP-reactive amino acids of SAP [1]. A conformational change of the protein part of SAP in relation with a different orientation of the desialylated oligosaccharide chain in comparison to the complete one is a possible explanation of our CIDNP results.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018570912192
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