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  • 1
    Electronic Resource
    Electronic Resource
    Separation of intramolecular NOE and exchange peaks in water exchange spectroscopy using spin-echo filters (1996)
    Springer
    Journal of biomolecular NMR 7 (1996), S. 77-82 
    Details
    ISSN: 1573-5001
    Keywords: Water exchange ; NOE ; Pulsed field gradients ; Macromolecules
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A technique for separating intramolecular NOE and solvent-proton exchange peaks in exchange spectroscopy is demonstrated. This method utilizes the large differences in relaxation and coupling properties of water and macromolecules to separate the two effects. The spin-echo filter consists of a water-frequency selective 90° pulse followed by a spin-echo sequence. If the echo time is sufficiently long, protein resonances (e.g. CαH protons) excited by the selective pulse are removed due to their much shorter T2 values and J-coupling evolution. By combining the filter with exchange spectroscopy (EXSY) or water exchange (WEX) filter experiments, exchange peaks can be selectively observed. In this paper the filter is combined with a modified version of the WEX filter (WEX II filter) with 1D and 2D detection and applied to a zinc finger peptide and to staphylococcal nuclease, allowing estimation of the contribution of intramolecular NOEs to the exchange spectra.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00190459
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A comparison of the immunogenicity of a pair of enantiomeric proteins (1993)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 16 (1993), S. 306-308 
    Details
    ISSN: 0887-3585
    Keywords: rubredoxin ; lgG antibody ; lgM antibody ; immunogen ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The immunogenicity of a folded, all D-amino acid protein- rubredoxin, has been compared with that for the corresponding L-protein enantiomer. Following multiple administrations with alum adjuvant, the L-protein induced a strong, specific lgG antibody response, whereas the D-protein did not. This relative lack of responsiveness to the D-protein cannot be attributed to rapid excretion, since it is retained at least 4 times longer than the natural L-protein. These observations provide the first direct evidence that a folded D-amino acid protein has low immunogenicity and is long lived in vivo. Proteins with such properties may be useful as molecular platforms in a variety of chemical and pharmaco-logical applications. © 1993 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340160309
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    Paper (German National Licenses)
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