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  • solid-phase peptide-synthesis  (2)
  • FK506 binding proteins  (1)
  • 1995-1999  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 269-276 
    ISSN: 1573-3904
    Keywords: metalloenzymes ; peptide-porphyrins ; solid-phase peptide-synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary New metal-tetraphenylporphyrins and Fmoc-lysine-metalloporphyrin derivatives have been used to prepare peptide-porphyrin and peptide-metalloporphyrin compounds via solid-phase peptide synthesis. A water-soluble peptide, covalently bound to a manganese(III)-porphyrin, has been used as a catalyst to promote the oxidation of ABTS by hydrogen peroxide ort-butylhydroperoxide.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 269-276 
    ISSN: 1573-3904
    Keywords: metalloenzymes ; peptide-porphyrins ; solid-phase peptide-synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract New metal-tetraphenylporphyrins and Fmoc-lysine-metalloporphyrin derivatives have been used to prepare peptide-porphyrin and peptide-metalloporphyrin compounds via solid-phase peptide synthesis. A water-soluble peptide, covalently bound to a manganese(III)-porphyrin, has been used as a catalyst to promote the oxidation of ABTS by hydrogen peroxide or t-butylhydroperoxide.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0006-3525
    Keywords: cyclic peptides ; molecular dynamics ; nmr ; conformation ; FK506 ; FK506 binding proteins ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational behavior in solution of a cyclic peptide with sequence cyclo-(Pro1-Pro2-Dab3 (cHexA)ψ[N7HCO]-Leu4ψ[NHCO]-Suc5-Gly6-) has been throughly investigated with the combined use of nmr and molecular dynamic techniques. The compound, which has been modeled to mimic the FK506 macrolide bound to the FK506 binding protein structure, can be considered as a peptidic analogue of the FK506 system.The synthesis was carried out on a phenylacetoamidomethyl resin using an appropriate protocol for the peptide chain elongation. The conformational properties of the cyclic hexapeptide were studied in DMSO and water. The nmr data in DMSO and restrained molecular dynamics simulations show the presence of two contiguous cis peptide bonds involving the -Gly-Pro-Pro- segment. This segment in water exhibits conformational heterogeneity presenting at least two distinct conformational families, characterized the first by cis-cis and the second by a trans-cis Gly-Pro-Pro configuration; the trans-cis isomer was fully characterized. © 1997 John Wiley & Sons, Inc. Biopoly 42: 349-361, 1997
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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