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Letters to Nature
Nature 200, 1006 - 1007 (07 December 1963); doi:10.1038/2001006a0

Proton Magnetic Relaxation and Protein Hydration

O. K.-DASZKIEWICZ, J. W. HENNEL, B. LUBAS & T. W. SZCZEPKOWSKI

Institute of Nuclear Physics, Polish Academy of Sciences.
Department of Physiological Chemistry, Medical Academy, Cracow, Poland.

WE have found that ovalbumin dissolved in water decreases the proton spin–lattice relaxation time T 1 and proton spin–spin relaxation time T 2 and we show that this effect is due to an increase of correlation time of part of the water molecules. The correlation time τ can be defined as the mean time of persistence of the angular position of a water molecule and is simply related1 to the Debye dielectric relaxation time τd, τ=τd/3. According to the theory of nuclear magnetic relaxation by Solomon2, T 1 and T 2 are functions of τ. In some cases τ can be expressed as a function of the macroscopic viscosity of the liquid1, but in the case of protein solutions such an explanation is not possible as was shown by Hennel et al. 3.

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  2. Solomon, I. , Phys. Rev., 99, 559 (1955). | Article | ISI | ChemPort |
  3. Hennel, J. W. , Hrynkiewicz, A. Z. , Krynicki, K. , Waluga, T. , and Zapalski, G. , Arch. Sci. (Geneva), 11, 243 (1958). | ChemPort |
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  7. Sheraga, H. A. , Protein Structure, 195 (Academic Press, New York, 1961).
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