Proton exchange and molecular orientation of water in hydrated collagen fibers: An NMR study of H2O and D2O

C. Migchelsen, H. J. C. Berendsen

    Research output: Contribution to journalArticleAcademicpeer-review

    115 Citations (Scopus)
    249 Downloads (Pure)


    An experimental study of proton and deuteron magnetic resonance of the hydration of collagen as a function of water content, temperature, and the addition of salts has been made. From the temperature dependency of linewidths, correlation times for molecular rotation of water molecules and proton exchange times have been determined. For a water content of 45 g H2O per 100 g collagen the rotational correlation time is 3× 10−8sec at 25 °C, with an activation energy of 4.8 kcal/mole, and the proton exchange time is 1.3 × 10−4sec with an activation energy of 10 kcal/mole. Ammonium ions increase the proton exchange rate. The proton exchange most probably occurs between proton donating and proton accepting groups on the macromolecule, intermediated by hydrogen‐bonded water molecules. It is shown that the exchange theory of Gutowsky, McCall, and Slichter is applicable to dipole coupling in anisotropic systems. From an analysis of the anisotropy of H2O and D2O rotation in terms of Saupe's parameters, is is concluded that a model with two specific water binding sites is consistent with experimental results.
    Original languageEnglish
    Pages (from-to)296-305
    Number of pages10
    JournalJournal of Chemical Physics
    Issue number1
    Publication statusPublished - 1973

    Cite this