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  • ionophore  (2)
  • Ion channel  (1)
  • Membrane proteins  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    European biophysics journal 22 (1993), S. 279-288 
    ISSN: 1432-1017
    Schlagwort(e): Gramicidin A ; Ion channel ; Membrane proteins ; FTIR ; Circular dichroism
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Physik
    Notizen: Abstract The structure of the channel-forming polypeptide gramicidin A (GA) incorporated into phosphatidylcholine (PC) liposomes has been studied as a function of the degree of unsaturation of the acyl chains of PC. The initial conformational state of GA in reconstituted bilayers is determined by the solvent in which the peptide and the lipid are initially co-dissolved, whereas the equilibrium conformational state (after heat incubation) is affected by the lipid structure rather than by the nature of the solvent. The conformational equilibrium of GA has been studied in liposomes prepared from PC having a variable number of double bonds in the fatty acid moiety, by circular dichroism and Fourier transform infrared. Liposomes were prepared from trifluoroethanol or ethanol solutions and incubated at 68°C. GA was shown to retain the conformation of the right-handed π $$\overleftarrow 6$$ .3 π $$\overrightarrow 6$$ .3 helix in PC with saturated acyl chains and with one double bond, whereas in dilinoleoyl-PC, having two double bond in each chain, the thermodynamically preferred structures are left-handed antiparallel and parallel double ππ5.6 helices. Natural soybean PC also favours left-handed ππ5.6 helical structures of GA (≈75%). This finding is discussed in terms of the role of PC unsaturation in the dynamic properties of the lipid matrix. Differences between observed FTIR spectra of the ↑↓ππ=5.6 helix in solution (and to a larger extent in the membrane) and the calculated IR spectra can be interpreted as resulting from deviation of the real structure from the theoretically derived ideal helix. The data obtained provide grounds for better understanding of a GA channel functioning in lipids of variable degrees of unsaturation.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 0006-3525
    Schlagwort(e): x-ray crystallography ; ionophore ; valinomycin analogue ; crystal and molecular structure ; Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: The crystal and molecular structure of the valinomycin analogue, cyclo [(D-Val-L-Lac-L-Ala-D-Hyi)2 (D-Val-L-Lac-L-Val-D-Hyi)] has been solved by x-ray direct methods using the “Shake and Bake” procedure. The crystals, grown from a mixture of octane/CH2Cl2, belong to space group P21 (Z = 4 ) with cell parameters a = 10.29, b = 32.08, c = 18.73 Å β = 97.05°, and contain two molecules per asymmetric unit. After anisotropic refinement the standard reliability factor was R1 = 0.058. The conformations of both independent molecules is similar to that observed for isoleucinomycin, cyclo [-(D-Ile-L-Lac-L-Ile-D-Hyi)3] [V. Z. Pletnev et al. (1980) Biopolymers, Vol. 19, pp. 1517-1534]. The structure has an asymmetric conformation stabilized by six intramolecular H bonds, five bonds being of the 4 → 1 type and one bond being of the 5 → 1 type. One water molecule is caged in the internal cavity of each cyclodepsipeptide. This conformation could represent an intermediate state between free and complexed forms of valinomycin. © 1997 John Wiley & Sons, Inc. Biopoly 42: 651-658, 1997
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    New York : Wiley-Blackwell
    Biopolymers 42 (1997), S. 645-650 
    ISSN: 0006-3525
    Schlagwort(e): valinomycin analogue ; ionophore ; x-ray direct methods ; structure and function ; Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: The conformation and intermolecular association of [D-Hyi2, L-Hyi4]meso-valinomycin {cyclo[-D-Val-D-Hyi-L-Val-L-Hyi- (D-Val-L-Hyi-L-Val-D-Hyi)2-], C60H102N6O18} in a crystal form obtained from ethanol solution has been determined by x-ray crystallography. Two depsipeptides and one ethanol molecule per asymmetric unit crystallize in space group P21 (Z = 4); a - 14.579, b = 39.795, c = 13.928 Å, β = 116.90, R1 = 0.0757. The molecular conformation is very similar to that observed in the trigonal P32 crystal form obtained from acetone solution [V. Z. Pletnev et al. (1991) Biopolymers, Vol. 31, pp. 409-415]. Both independent molecules in the crystal adopt a similar distorted bracelet structure with a sterically inaccessible, partially formed, ion-binding center that is stabilized by six 4 → 1 type H bonds. The observed conformation accounts for the inability of the molecule to complex ions. Close examination of the three crystallographically independent molecules reveals that differences in the backbone conformation associated with solvent interaction are significantly larger than those associated with hydrophobic van der Waals interactions of crystal packing.© 1997 John Wiley & Sons, Inc. Biopoly 42: 645-650, 1997
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
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