ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1572-8854
    Keywords: Gallium ; porphyrinato ; acetate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The title compound, Ga(tpp)(OAc), crystallizes in the space group P21/n witha=10.628(2),b=16.176(2),c=20.750(2), Å, β=92.64(2)°, andZ=4. The gallium atom has a squarepyramidal coordination geometry formed by the four nitrogen atoms of the porphyrinato group (Np) and the acetate ion. The geometry around the gallium center of the Ga(tpp)(OAc) molecule has Ga−O(1)=1.874(4) Å and average Ga−Np(porphyrin nitrogen)=2.056(4) Å. The acetate group is unidentately coordinated to the gallium (III) atom. Ga-71 NMR spectroscopy provides a complementary method for investigation of the acetate ligand. Combining the calculated value of τc, 29.0 ps, with the measured Ga-71 quadrupolar relaxation time, T1Q=11.1 μs, the quadrupole coupling constant of Ga-71 is 28.1 MHz. This further supports that Ga is covalently coordinated to the acetate and tpp in Ga(tpp)(OAc). The methyl and carbonyl carbons of the acetate group are separately located at 20.4 and 168.8 ppm at 24°C for the Ga(tpp)(OAc).
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 3 (1996), S. 3-16 
    ISSN: 1573-3904
    Keywords: Cell adhesion ; Collagen ; Peptide amphiphiles ; Triple-helical peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The triple-helical conformation of collagen has been proposed to be important for mediation of cellular activities, such as adhesion and activation, extracellular matrix assembly, and enzyme function. We have developed synthetic protocols that allow for the study of biological activities of specific collagen sequences in triple-helical conformation. These methods primarily involve solid-phase assembly and covalent linkage of three peptide chains. The resultant triple-helical peptides have sufficient thermal stabilities to permit structural and biological characterization under physiological conditions. The present article critically reviews the various approaches for constructing synthetic triple-helices.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...