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  • solid-phase peptide-synthesis  (2)
  • 2D NMR  (1)
  • Biochemistry and Biotechnology  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Evaluation of errors of interproton distances and correlation time determined from NMR cross-relaxation rates (1992)
    Springer
    Journal of biomolecular NMR 2 (1992), S. 573-582 
    Details
    ISSN: 1573-5001
    Keywords: Amaninamide ; Correlation time ; Evaluation of errors ; Interproton distances ; NOESY ; ROESY ; 2D NMR ; Peptides ; Cross-relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We have analyzed a combined use of the two-dimensional nuclear Overhauser effect in the laboratory frame (NOESY) and in the rotating frame (ROESY) to determine interproton distances and correlation time in medium-sized rigid molecules (Davis, 1987). This method can be applied in the intermediate motional regime, 0.2 〈 ωoτc, 〈 5, (τc, correlation time, (ωo resonance frequency). Error limits depend on the motional regime and are smallest near ωoτc=1.14. The method was tested on six geminal proton pairs in the bicyclic octapeptide (S-deoxo-γ-[R]-OH-Ile3 amaninamide, Mw =870) for which at 297 K in DMSO, a correlation time of 1.0 ns, with a standard deviation of 0.12 ns, and an interproton distance of 1.87 Å, with standard deviation of 0.04 Å, are obtained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02192846
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  • 2
    Electronic Resource
    Electronic Resource
    New synthetic tools for peptide-tetraphenylporphyrin derivatives (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 269-276 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02443544
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  • 3
    Electronic Resource
    Electronic Resource
    New Synthetic Tools for Peptide-Tetraphenylporphyrin Derivatives (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 269-276 
    Details
    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
    URL: http://dx.doi.org/10.1023/A:1008869818565
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  • 4
    Electronic Resource
    Electronic Resource
    Conformational behaviour of A cyclolinopeptide a analogue: Two-dimensional NMR study of cyclo(Pro1-Pro-Phe-Phe-Ac6c-IIe-ala-Val8) (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 330-340 
    Details
    ISSN: 1075-2617
    Keywords: Cyclolinopeptide A ; cyclooctapeptides ; NMR ; conformational studies ; restrained molecular dynamics ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The cyclic octapeptide cyclo[-Pro1-Pro-Phe-Phe-Ac6c-Ile-ala-Val8-] [C8-Ac6c], containing the Pro1-Pro-Phe-Phe sequence, followed by a bulky helicogenic Cα,α-dialkylated glycine residue Ac6c (1-aminocyclohexane-1-carboxylic acid), and a D-Ala residue at position 7 has been synthesized. This cyclic peptide is a deletion analogue of the naturally occurring cyclic nonapeptide cyclolinopeptide A (CLA). It has been designed with the aim of studying the role that the Ac6c and D-Ala residues play on the conformational behaviour of the whole molecule and their influence on the conformation of the Pro1-Pro-Phe-Phe sequence when compared with cyclolinopeptide A.C8Ac6c has been investigated in chloroform and acetonitrile solutions by 2D NMR techniques. Only one set of sharp signals is observed in both solvents. This evidence strongly supports the hypothesis that only one conformational state exists in the chosen solvents. The interpretation of the experimental data points to the existence for C8-Ac6c of a very rigid structure stabilized by intramolecular hydrogen bonds. The measured NOE effects allow the calculation of internuclear distances, which have been used as restraints in molecular dynamic calculations. The proposed conformation of the molecule shows that the Pro-Pro-Phe segment retains the conformation observed in natural CLA both in solution and in the solid state and that the Ac6c residue indeed reinforces the ring rigidity not permitting the formation of any appropriate cavity in which inorganic cations could be complexed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010508
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