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).
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© 1986 Birkhäuser Boston, Inc.
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Spisni, A., Gotsis, E.D., Ponnusamy, E., Fiat, D. (1986). 17O NMR as a Probe to Study Hydration and Hydrogen Bonding of Amino Acids and Polypeptides. In: Niccolai, N., Valensin, G. (eds) Advanced Magnetic Resonance Techniques in Systems of High Molecular Complexity. Progress in Inorganic Biochemistry and Biophysics, vol 2. Birkhäuser Boston. https://doi.org/10.1007/978-1-4615-8521-3_4
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DOI: https://doi.org/10.1007/978-1-4615-8521-3_4
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