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  • 1
    Electronic Resource
    Electronic Resource
    Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy (1991)
    Springer
    Journal of biomolecular NMR 1 (1991), S. 167-173 
    Details
    ISSN: 1573-5001
    Keywords: Channel structure ; Magainin ; Acetylcholine receptor ; Lipid bilayer ; Amphiphilic α-helix ; 15N chemical shift ; Solid-state NMR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Solid-state NMR spectroscopy was used to determine the orientations of two amphipathic helical peptides associated with lipid bilayers. A single spectral parameter provides sufficient orientational information for these peptides, which are known, from other methods, to be helical. The orientations of the peptides were determined using the15N chemical shift observed for specifically labeled peptide sites. Magainin, an antibiotic peptide from frog skin, was found to lie in the plane of the bilayer. M2δ, a helical segment of the nicotinic acetylcholine receptor, was found to span the membrane, perpendicular to the plane of the bilayer. These findings have important implications for the mechanisms of biological functions of these peptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01877228
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  • 2
    Electronic Resource
    Electronic Resource
    Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers (1995)
    Springer
    Journal of biomolecular NMR 6 (1995), S. 329-334 
    Details
    ISSN: 1573-5001
    Keywords: Solid-state NMR ; Magainin ; Membranes ; Oriented samples ; Structure determination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A three-dimensional 1H chemical shift/1H-15N dipolar coupling/15N chemical shift correlation spectrum was obtained on a sample of specifically 15N-labeled magainin peptides oriented in lipid bilayers between glass plates in a flat-coil probe. The spectrum showed complete resolution of the resonances from two labeled amide sites in all three dimensions. The three orientationally dependent frequencies associated with each resonance enabled the orientation of the peptide planes to be determined relative to the direction of the applied magnetic field. These results demonstrate the feasibility of multiple-pulse spectroscopy in a flat-coil probe, the ability to measure three spectral parameters from each site in a single experiment, and the potential for resolving among many labeled sites in oriented membrane proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197814
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Comparison of the dynamics of the membrane-bound form of fd coat protein in micelles and in bilayers by solution and solid-state nitrogen-15 nuclear magnetic resonance spectroscopy (1988)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 4 (1988), S. 123-130 
    Details
    ISSN: 0887-3585
    Keywords: NMR spectroscopy ; protein dynamics ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Solid-state and solution 15N nuclear magnetic resonance experiments on uniformly and specifically 15N labeled coat protein in phospholipid bilayers and in detergent micelles are used to describe the dynamics of the membrane-bound form of the protein. The residues in the N- and C-terminal portions of the coat protein in both phospholipid bilayers and in detergent micelles are mobile, while those in the hydrophobic midsection are immobile. There is evidence for a gradient of mobility in the C-terminal region of the coat protein in micelles; at 25°C only the last two residues are mobile on the 109-Hz timescale, while the last six to eight residues appear to be mobile on slower timescales and highly mobile at higher temperatures. Since all of the C-terminal residues are immobile in the virus particles, the mobility of these residues in the membrane-bound form of the protein may be important for the formation of protein-DNA interactions in the assembly process.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340040205
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    Paper (German National Licenses)
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