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  • 1
    Electronic Resource
    Electronic Resource
    Crystallographic structure of a helical lipopeptaibol antibiotic analogue (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 213-218 
    Details
    ISSN: 1573-3904
    Keywords: α/310-Helix〉 ; Nitroxide amino acid ; Peptide conformation ; X-ray diffraction ; α-Tetrasubstituted amino acids ; Trichogin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An X-ray diffraction analysis of the [Fmoc0,TOAC4,8, Leu-OMe11] analogue of thelipopeptaibol antibiotic trichogin A IV shows that the undecapeptide isfolded in a right-handed, mixed α/310-helix. The helicalmolecules are connected in a head-to-tail arrangement along the b-axisthrough C=O···H-N intermolecular H-bonding. Thispacking mode generates a hydrophobic cavity where the FmocNα-protecting groups are accommodated. The distances andangles between the nitroxide groups of the two TOAC residues, separated byone turn of the α-helix, have been determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008874816982
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  • 2
    Electronic Resource
    Electronic Resource
    The polypeptide 310-helix as a template and a spacer (1995)
    Springer
    International journal of peptide research and therapeutics 2 (1995), S. 187-189 
    Details
    ISSN: 1573-3904
    Keywords: β-turns ; Cα-tetrasubstituted α-amino acids ; Conformational restrictions ; Peptide conformation ; X-ray diffraction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary X-ray diffraction analyses have provided detailed structural information on the 310-helices of (i) pBrBz-d-(αMe)Phe-(Aib)2-d-(αMe)Phe-Aib-OtBu and Ac-(Aib)2-l-Lys(Bz)-(Aib)2-l-Lys(Bz)-(Aib)2-NHMe as suitable templates for molecular recognition studies, and (ii) pBrBz-TOAC-(l-Ala)2-TOAC-l-Ala-NHtBu as an appropriate spacer for an ESR study of side chain to side chain interactions. In addition, in Ac-TOAC-(Aib)2-l-Trp-Aib-OMe, forming a 310-helix, the TOAC residue plays the role of an effective quencher of the fluorescence of the tryptophan residue located one turn apart.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00119149
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallographic structure of a helical lipopeptaibol antibiotic analogue (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 213-218 
    Details
    ISSN: 1573-3904
    Keywords: α/310-Helix ; Nitroxide amino acid ; Peptide conformation ; X-ray diffraction ; α-Tetrasubstituted amino acids ; Trichogin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary An X-ray diffraction analysis of the [Fmoc0, TOAC4,8, Leu-OMe11]analogue of the lipopeptaibol antibiotic trichogin A Iv shows that the undecapeptide is folded in a right-handed, mixed α/310-helix. The helical molecules are connected in a head-to-tail arrangement along the b-axis through C=O...H-N intermolecular H-bonding. This packing mode generates a hydrophobic cavity where the Fmoc Nα-protecting groups are accommodated. The distances and angles between the nitroxide groups of the two TOAC residues, separated by one turn of the α-helix, have been determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02442878
    Location Call Number Expected Availability
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    Paper (German National Licenses)
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