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. 1990 Nov;58(5):1183–1197. doi: 10.1016/S0006-3495(90)82459-0

Fluctuations, exchange processes, and water diffusion in aqueous protein systems

A study of bovine serum albumin by diverse NMR techniques

R Kimmich 1, T Gneiting 1, K Kotitschke 1, G Schnur 1
PMCID: PMC1281063  PMID: 19431772

Abstract

Experimental frequency, concentration, and temperature dependences of the deuteron relaxation times T1 and T2 of D2O solutions of bovine serum albumin are reported and theoretically described in a closed form without formal parameters. Crucial processes of the theoretical concept are material exchange, translational diffusion of water molecules on the rugged surfaces of proteins, and tumbling of the macromolecules. It is also concluded that, apart from averaging of the relaxation rates in the diverse deuteron phases, material exchange contributes to transverse relaxation by exchange modulation of the Larmor frequency. The rate limiting factor of macromolecular tumbling is determined by the free water content. In a certain analogy to the classical free-volume theory, a “free-water-volume theory” is presented. There are two characteristic water mass fractions indicating the saturation of the hydration shells (Cs ≈ 0.3) and the onset of protein tumbling (C0 ≈ 0.6). The existence of the translational degrees of freedom of water molecules in the hydration shells has been verified by direct measurement of the diffusion coefficient using an NMR field-gradient technique. The concentration and temperature dependences show phenomena indicating a percolation transition of clusters of free water. The threshold water content was found to be Ccw ≈ 0.43.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Careri G., Giansanti A., Rupley J. A. Proton percolation on hydrated lysozyme powders. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6810–6814. doi: 10.1073/pnas.83.18.6810. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Careri G, Giansanti A, Rupley JA. Critical exponents of protonic percolation in hydrated lysozyme powders. Phys Rev A Gen Phys. 1988 Apr 1;37(7):2703–2705. doi: 10.1103/physreva.37.2703. [DOI] [PubMed] [Google Scholar]
  3. Civan M. M., Achlama A. M., Shporer M. The relationship between the transverse and longitudinal nuclear magnetic resonance relaxation rates of muscle water. Biophys J. 1978 Feb;21(2):127–136. doi: 10.1016/S0006-3495(78)85513-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Civan M. M., Shporer M. Pulsed nuclear magnetic resonance study of 17-O, 2-D, and 1-H of water in frog striated muscle. Biophys J. 1975 Apr;15(4):299–306. doi: 10.1016/S0006-3495(75)85820-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Clark M. E., Burnell E. E., Chapman N. R., Hinke J. A. Water in barnacle muscle. IV. Factors contributing to reduced self-diffusion. Biophys J. 1982 Sep;39(3):289–299. doi: 10.1016/S0006-3495(82)84519-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fuller M. E., 2nd, Brey W. S., Jr Nuclear magnetic resonance study of water sorbed on serum albumin. J Biol Chem. 1968 Jan 25;243(2):274–280. [PubMed] [Google Scholar]
  7. Fung B. M. Proton and deuteron relaxation of muscle water over wide ranges of resonance frequencies. Biophys J. 1977 May;18(2):235–239. doi: 10.1016/S0006-3495(77)85610-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gallier J., Rivet P., de Certaines J. 1H- and 2H-NMR study of bovine serum albumin solutions. Biochim Biophys Acta. 1987 Sep 2;915(1):1–18. doi: 10.1016/0167-4838(87)90119-1. [DOI] [PubMed] [Google Scholar]
  9. Held G., Noack F., Pollak V., Melton B. Protonenspinrelaxation und Wasserbeweglichkeit in Muskelgewebe. Z Naturforsch C. 1973 Jan-Feb;28(1):59–62. [PubMed] [Google Scholar]
  10. Kasturi S. R., Hazlewood C. F., Yamanashi W. S., Dennis L. W. Evidence for chemically shifted water in the brine shrimp, (Artemia): possible interpretations. Physiol Chem Phys Med NMR. 1983;15(1):5–11. [PubMed] [Google Scholar]
  11. Koenig S. H., Hallenga K., Shporer M. Protein-water interaction studied by solvent 1H, 2H, and 17O magnetic relaxation. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2667–2671. doi: 10.1073/pnas.72.7.2667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Koenig S. H., Schillinger W. E. Nuclear magnetic relaxation dispersion in protein solutions. I. Apotransferrin. J Biol Chem. 1969 Jun 25;244(12):3283–3289. [PubMed] [Google Scholar]
  13. Korb J, Gouyet J. Diffusion and spin correlation in fractal percolation clusters. Phys Rev B Condens Matter. 1988 Jul 1;38(1):493–499. doi: 10.1103/physrevb.38.493. [DOI] [PubMed] [Google Scholar]
  14. Kuntz I. D., Jr, Kauzmann W. Hydration of proteins and polypeptides. Adv Protein Chem. 1974;28:239–345. doi: 10.1016/s0065-3233(08)60232-6. [DOI] [PubMed] [Google Scholar]
  15. Kärger J, Pfeifer H, Vojta G. Time correlation during anomalous diffusion in fractal systems and signal attenuation in NMR field-gradient spectroscopy. Phys Rev A Gen Phys. 1988 Jun 1;37(11):4514–4517. doi: 10.1103/physreva.37.4514. [DOI] [PubMed] [Google Scholar]
  16. O'Shaughnessy B, Procaccia I., I Analytical solutions for diffusion on fractal objects. Phys Rev Lett. 1985 Feb 4;54(5):455–458. doi: 10.1103/PhysRevLett.54.455. [DOI] [PubMed] [Google Scholar]
  17. Orbach R. Dynamics of fractal networks. Science. 1986 Feb 21;231(4740):814–819. doi: 10.1126/science.231.4740.814. [DOI] [PubMed] [Google Scholar]
  18. Packer K. J. The dynamics of water in heterogeneous systems. Philos Trans R Soc Lond B Biol Sci. 1977 Mar 29;278(959):59–87. doi: 10.1098/rstb.1977.0031. [DOI] [PubMed] [Google Scholar]
  19. Pauls K. P., MacKay A. L., Söderman O., Bloom M., Tanjea A. K., Hodges R. S. Dynamic properties of the backbone of an integral membrane polypeptide measured by 2H-NMR. Eur Biophys J. 1985;12(1):1–11. doi: 10.1007/BF00254089. [DOI] [PubMed] [Google Scholar]
  20. Peemoeller H., Yeomans F. G., Kydon D. W., Sharp A. R. Water molecule dynamics in hydrated lysozyme. A deuteron magnetic resonance study. Biophys J. 1986 Apr;49(4):943–948. doi: 10.1016/S0006-3495(86)83722-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Schauer G., Kimmich R., Nusser W. Deuteron field-cycling relaxation spectroscopy and translational water diffusion in protein hydration shells. Biophys J. 1988 Mar;53(3):397–404. doi: 10.1016/S0006-3495(88)83116-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Usha M. G., Wittebort R. J. Orientational ordering and dynamics of the hydrate and exchangeable hydrogen atoms in crystalline crambin. J Mol Biol. 1989 Aug 20;208(4):669–678. doi: 10.1016/0022-2836(89)90157-5. [DOI] [PubMed] [Google Scholar]

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