17O NMR as a Probe to Study Hydration and Hydrogen Bonding of Amino Acids and Polypeptides

  • A. Spisni
  • E. D. Gotsis
  • E. Ponnusamy
  • D. Fiat
Chapter
Part of the Progress in Inorganic Biochemistry and Biophysics book series (PIBB, volume 2)

Abstract

The conformation of amino acids and polypeptides is known to play a crucial role in the modulation of their biological activity. Several investigators have indicated that solute-solvent and solute-solute interactions are responsible for the modifications as well as the stabilization of the solute conformation (1,2) and that intra- and intermolecular hydrogen bonding is the principal route through which these interactions take place (3,4).

Keywords

Chemical Shift Inter Molecular Hydrogen Bond Solute Conformation Principal Route Anionic Amino Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Birkhäuser Boston, Inc. 1986

Authors and Affiliations

  • A. Spisni
    • 1
    • 2
  • E. D. Gotsis
    • 1
    • 2
  • E. Ponnusamy
    • 1
    • 2
  • D. Fiat
    • 1
    • 2
  1. 1.Istituto di Chimica BiologicaUniversità di ParmaParmaItaly
  2. 2.Dept. of Physiology and Biophysics, College of MedicineUniversity of Illinois at ChicagoChicagoUSA

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