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  • 1995-1999  (4)
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Macromolecules 28 (1995), S. 1547-1551 
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1520-5827
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 38 (1996), S. 557-566 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The molecular and crystal structure of curdlan triacetate, acetylated (1 → 3)β-D-glucan, was analyzed by means of an x-ray diffraction technique with the help of the linked-atom least-squares method. Unit cell dimensions are a = b = 11.00(1), c(fiber axis) = 22.91 (9) Å, and γ = 120°. The space group is P61. The unit cell contains six chemical repeating units related by 6/I-helical symmetry, which is essentially the same as the backbone conformation of one of the modifications (form I) of curdlan. During the refinement calculation, the terminal methyl in every acetyl moiety was elastically restrained to the trans conformation commonly observed in related oligosaccharide structures. The difference Fourier map, the observed and calculated densities, and the thermogravimetric measurement indicated one water molecule per glucose residue. The water oxygen is linked to two carbonyl oxygens in adjacent molecules by hydrogen bonds. The conformation of the primary acetyl moiety is a (skew, -gauche, trans). So far, no skew conformation was observed for the primary acetyl and hydroxyl moieties except in α, β-panose. In both cases, the unusual eclipsed orientation of the primary group is attributed to the hydrogen bond and this conformation is quite different from that of pachyman triacetate. © 1996 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 40 (1996), S. 85-103 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Recent x-ray structure analyses of peptides in Japan were reviewed. A series of peptides containing an aminoisobutyric acid (Aib) residue was analyzed and their helical types were investigated. Two convenient methods to determine helical types were obtained. One method was obtained by calculating averaged helical parameters and the other was obtained by investigating meridional intensity distributions. The conformations of some peptides, such as aureobasidin E, ascidiacyclamide, synthetic analogues of heat-stable enterotoxin, were studied by an x-ray diffraction method, and in some cases, with the help of nmr spectroscopy and molecular mechanics calculations. Since these peptides have physiologically important activities, the structure-activity relationships of these peptides were discussed. Several other peptide structures and the polymorphism of amino acids are also reported. © 1996 John Wiley & Sons, Inc.
    Additional Material: 19 Ill.
    Type of Medium: Electronic Resource
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