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  • 1995-1999  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Zinc Finger Domains: From Predictions to Design (1995)
    s.l. : American Chemical Society
    Accounts of chemical research 28 (1995), S. 14-19 
    Details
    ISSN: 1520-4898
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ar00049a003
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    LESSONS FROM ZINC-BINDING PEPTIDES (1997)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biophysics and Biomolecular Structure 26 (1997), S. 357-371 
    Details
    ISSN: 1056-8700
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Physics
    Notes: Abstract Zinc-finger domains are small metal-binding modules that are found in a wide range of gene regulatory proteins. Peptides corresponding to these domains have provided valuable model systems for examining a number of biophysical parameters entirely unrelated to their nucleic acid binding properties. These include the chemical basis for metal-ion affinity and selectivity, thermodynamic properties related to hydrophobic packing and beta-sheet propensities, and constraints on the generation of ligand-binding and potential catalytic sites. These studies have laid the foundation for applications such as the generation of optically detected zinc probes and the design of metal-binding peptides and proteins with desired spectroscopic and chemical properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.biophys.26.1.357
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    A 2.2 Å resolution crystal structure of a designed zinc finger protein bound to DNA (1996)
    [s.l.] : Nature Publishing Group
    Nature structural biology 3 (1996), S. 940-945 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Considerable recent effort has been devoted to the design and selection of sequence-specific DNA binding proteins based on tandem arrays of Cys2His2 zinc finger domains. While the DNA binding properties of these designed proteins have been studied extensively, the structural basis for site-specific ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb1196-940
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Letting your fingers do the walking (1997)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 15 (1997), S. 323-323 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Even before the first three-dimensional structures of DNA binding proteins were determined, it was hoped that simple relationships might exist between the amino acid residues used for sequence-specific nucleic acid recognition and the nucleotide bases that these residues contact. With the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0497-323
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    Paper (German National Licenses)
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  • 5
    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)
    Fulltext
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