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  • Hydrogen bonding  (1)
  • Sulfonate salt  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 1 (1994), S. 127-133 
    ISSN: 1573-3904
    Keywords: Conformation ; Crystallization ; Hydrogen bonding ; Sulfonate salt ; X-ray structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Continuing a line of investigations on methods for formation and growth of high-quality crystals of peptides, the glycylglycine sequence has been crystallized by evaporation methods as a salt with 1,5-naphthalenedisulfonic acid. The structure of the peptide is highly extended, and is conformationally quite similar to the structures which have been characterized for other zwitterionic and salt forms of this sequence. Thus, crystallization as a salt with this sulfonic acid has imposed no undue influence upon the molecular conformation. These results offer further indication that the preparation of peptide sulfonate salts, particularly with arene templates, may have broad general utility for crystallization of interesting sequences which until now have not been approachable in their zwitterionic forms.
    Type of Medium: Electronic Resource
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