Proton exchange rates from amino acid side chains - Implications for image contrast

Magnetic Resonance in Medicine

Volumn 35, Issue 1, 1996, Pages 30-42

  Liepinsh, Edvards ^a   Otting, Gottfried ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

cross relaxation; image contrast; magnetization exchange; proton exchange

Indexed keywords

AMINO ACIDS; BIOMOLECULES; MAGNETIC RESONANCE IMAGING; MAGNETIZATION; MOLECULES;

CROSS RELAXATION; CROSS RELAXATION RATES; EXCHANGEABLE PROTONS; IMAGE CONTRASTS; MAGNETIZATION EXCHANGE; MAGNETIZATION TRANSFER; PHYSIOLOGICAL CONCENTRATIONS; PROTON EXCHANGE;

FINANCE;

AMINO ACID; ARGININE; CARBONIC ACID; LYSINE; PHOSPHATE; SERINE; THREONINE; TYROSINE; WATER;

ARTICLE; CATALYSIS; CONTRAST; MAGNETISM; NUCLEAR MAGNETIC RESONANCE; PH; PROTON TRANSPORT;

EID: 0030051552     PISSN: 07403194     EISSN: None     Source Type: Journal    
DOI: 10.1002/mrm.1910350106     Document Type: Article

References (58)

1. S. D. Wolff, R. S. Balaban, Magnetization transfer contrast (MTC) and tissue water proton relaxation in vivo. Magn. Reson. Med. 10, 135-144 (1989).
2. J. C. Gore, M. S. Brown, J. Zhong, K. F. Mueller, W. Good, NMR relaxation of water in hydrogel polymers: a model for tissue. Magn. Reson. Med. 9, 325-332 (1989).
3. S. H. Koenig, R. D. Brown III. Field-cycling relaxometry of protein solutions and tissue: implications for MRI. Prog. NMR Spectr. 22, 487-567 (1990).
4. S. H. Koenig, R. D. Brown III, R. Ugolini, A unified view of relaxation in protein solutions and tissue, including hydration and magnetization transfer. Magn. Reson. Med. 29, 77-83 (1993).
5. S. H. Koenig, R. D. Brown III, A molecular theory of relaxation and magnetization transfer: application to cross-linked BSA, a model for tissue. Magn. Reson. Med. 30, 685-695 (1993).
6. B. P. Hills. The proton exchange cross-relaxation model of water relaxation in biopolymer systems. Mol. Phys. 76, 489-508 (1992).
7. B. P. Hills, The proton exchange cross-relaxation model of water relaxation in biopolymer systems. 2. The sol and gel states of gelatin. Mol. Phys. 76, 509-523 (1992).
8. T. D. Scholz, T. L. Ceckler, R. S. Balaban, Magnetization transfer characterization of hypertensive cardiomyopathy: significance of tissue water content. Magn. Reson. Med. 29, 352-357 (1993).
9. J. Zhong, J. C. Gore, I. M. Armitage, Relative contributions of chemical exchange and other relaxation mechanisms in protein solutions and tissues. Magn. Reson. Med. 11, 295-308 (1989).
10. T. A. Fralix, T. L. Ceckler, S. D. Wolff, S. A. Simon, R. S. Balaban, Lipid bilayer and water proton magnetization transfer: effect of cholesterol. Magn. Reson. Med. 18, 214-223 (1991).
11. J. Grad, R. G. Bryant, Nuclear magnetic cross-relaxation spectroscopy. J. Magn. Reson. 90, 1-8 (1990).
12. M. Iino, Dynamic properties of bound water studied through macroscopic water relaxations in concentrated protein solutions. Biochem. Biophys. Acta 1208, 81-88 (1994).
13. 1H magnetization transfer imaging in vivo. Magn. Reson. Med. 17, 304-314 (1991).
14. H. McIlwain, H. S. Bachelard, "Biochemistry and the Central Nervous System," Churchill Livingstone, Edinburgh, 1985.
15. G. Otting, E. Liepinsh, K. Wüthrich, Protein hydration in aqueous solution. Science 254, 974-980 (1991).
16. E. Liepinsh, G. Otting, K. Wüthrich. NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins. J. Biomol. NMR 2, 447-465 (1992).
17. E. Liepinsh, G. Otting, K. Wüthrich, NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution. Nucl. Acid. Res. 20, 6549-6553 (1992).
18. L. T. Kakalis, I. C. Baianu, Oxygen-17 and deuterium nuclear magnetic relaxation studies of lysozyme hydration in solution: field dispersion, concentration, pH/pD, and protein activity dependencies. Arch. Biochem. Biophys. 287, 829-841 (1988).
19. V. P. Denisov, B. Halle. Protein hydration dynamics in aqueous solution: a comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion. J. Mol. Biol. 245, 682-697 (1995).
20. V. P. Denisov, B. Halle, Hydrogen exchange and protein hydration: the deuteron spin relaxation dispersions of BPTI and ubiquitin. J. Mol. Biol. 245, 698-709 (1995).
21. A. C. Barnes, T. W. N. Bieze, J. E. Enderby, J. C. Leyte, Dynamics of water in the poly(ethylene oxide) hydration shell: a quasi elastic neutron-scattering study. J. Phys. Chem. 98, 11527-11532 (1994).
22. R. M. Brunne, E. Liepinsh, G. Otting, K. Wüthrich, W. F. van Gunsteren, Hydration of proteins: a comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations. J. Mol. Biol. 231, 1040-1048 (1993).
23. G. Otting, K. Wüthrich, Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules. J. Am. Chem. Soc. 111, 1871-1875 (1989).
24. M. Eigen, Protonenübertragung, säure-base-katalyse und enzymatische hydrolyse. Teil I: elementarvorgänge. Angew. Chemie 12, 489-588 (1963).
25. 1H NMR-Studien," Ph.D. thesis No. 5992, ETH-Zürich, 1977.
26. K. Wüthrich, "NMR of Proteins and Nucleic Acids," Wiley, New York, 1986.
27. Z. Luz, S. Meiboom, Rate and mechanism of proton exchange in aqueous solutions of phosphate buffer. J. Chem. Phys. 86, 4764-4766 (1964).
28. D. Lankhorst, J. Schriever, J. C. Leyte, An NMR relaxation study of hydrogen exchange and its deuterium isotope effects in aqueous carboxylic acid solutions. Chem. Phys. 77, 319-340 (1983).
29. E. K. Ralph, E. Grunwald, Proton exchange and solvation of imidazole in t-butyl alcohol-water mixtures. J. Am. Chem. Soc. 91, 2429-2432 (1969).
30. Z. Luz, S. Meiboom. Kinetics of proton exchange in aqueous solutions of acetate buffer. J Chem. Phys. 39, 3923-3925 (1963).
31. 2O. Can. J. Chem. 41, 2477-2481 (1963).
32. R. F. Schmidt, G. Thews, "Human Physiology," 2nd. ed., Springer Verlag, Berlin, 1989.
33. D. D. Perrin, "Dissociation Constants of Inorganic Acids and Bases in Aqueous Solution." Butterworth, London, 1969.
34. R. M. C. Dawson, D. C. Elliott, W. H. Elliott, K. M. Jones, "Data for Biochemical Research," Clarendon, Oxford, 1986.
35. K. Roth, B. Huebsch, D. J. Meyerhoff, S. Naruse, J. R. Gober, T. J. Lawry, M. D. Boska, G. B. Matson, M. W. Weiner, Noninvasive quantitation of phosphorous metabolites in human tissue by NMR spectroscopy. J. Magn. Reson. 81, 299-311 (1989).
36. W. F. Ganong, "Review of Medical Physiology," LANGE Medical Publications, Los Altos, 1983.
37. S. W. Englander, N. W. Downer, H. Teitelbaum, Hydrogen exchange. Annu. Rev. Biochem. 41, 903-924 (1972).
38. E. Grunwald, K. C. Chang, P. L. Skipper, V. K. Anderson. Kinetics of bifunctional proton transfer. 2. Lysine and cysteine in aqueous solutions. J. Phys. Chem. 80, 1425-1431 (1976).
39. Y. Bai, J. S. Milne, L. Mayne, S. W. Englander, Primary structure effects on peptide group hydrogen exchange. Proteins 17, 75-86 (1993).
40. P. Plateau, M. Guéron, Exchangeable proton NMR without baseline distortion using new strong-pulse sequences. J. Am. Chem. Soc. 104, 7310-7311 (1982).
41. 1H NMR experiments. J. Biomol. NMR 1, 209-215 (1991).
42. G. Otting, E. Liepinsh, K. Wüthrich, Polypeptide hydration in mixed solvents at law temperatures. J. Am. Chem. Soc. 114, 7093-7095 (1992).
43. T. M. Devlin, "Textbook of Biochemistry," 3rd ed., Wiley, New York, 1992.
44. S. W. Englander, N. R. Kallenbach, Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16, 521-655 (1983).
45. K. D. Berndt, J. Beunink, W. Schröder, K. Wüthrich, Designed replacement of an internal hydration water molecule in BPTI: structural and functional implications of a glycineto-serine mutation. Biochemistry 32, 4564-4570 (1993).
46. E. Liepinsh, K. D. Berndt, R. Sillard, V. Mutt, G. Otting, Solution structure and dynamics of PEC-60, a protein of the Kazal type inhibitor family, determined by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 239, 137-153 (1994).
47. G. Wagner, K. Wüthrich, Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance. J. Mol. Biol. 160, 343-361 (1982).
48. T. L. Ceckler, R. S. Balaban, Tritium-proton magnetization transfer as a probe of cross relaxation in aqueous lipid bilayer suspensions. J. Magn. Reson. 93, 572-588 (1991).
49. 2O. Solvent saturation and chemical exchange in superoxide dismutase. FEBS Lett. 91. 320-324 (1978).
50. A. Kalk, H. J. C. Berendsen. Proton magnetic relaxation and spin diffusion in proteins. J. Magn. Reson. 24, 343-366 (1976).
51. K. Abdolall, A. L. MacKay, M. Bloom. The lipid-water interaction in sodium laurate. J. Magn. Reson. 29, 309-317 (1978).
52. P. Caravatti, M. H. Levitt, R. R. Ernst, Selective excitation in solid-state NMR in the presence of multiple-pulse line narrowing. J. Magn. Reson. 68, 323-334 (1986).
53. J. Hu, C. Ye, A simple approach to measuring spin diffusion of abundant nuclei in dipolar-broadened solids. J. Magn. Reson. 99, 576-581 (1992).
54. . J. Grad, D. Mendelson, F. Hyder, R. G. Bryant, Direct measurements of longitudinal relaxation and magnetization transfer in heterogeneous systems. J. Magn. Reson. 86, 416-419 (1990).
55. M. Ernst, R. R. Ernst, Heteronuclear dipolar cross-correlated cross relaxation for the investigation of side-chain motions. J. Magn. Reson. A 110, 202-213 (1994).
56. 19F NMR investigation of molecular motion and packing in sonated phospholipid vesicles. Biochemistry 24, 7153-7161 (1985).
57. F. J. M. van de Ven, H. G. J. M. Janssen, A. Gräslund, C. W. Hilbers, Chemically relayed nuclear Overhauser effects. Connectivities between resonances of nonexchangeable protons and water. J. Magn. Reson. 79, 221-235 (1988).
58. H. Fritzsche, L. Kan, K. Weller, W. Scheiding, J. R. Kast, P. O. P. Ts'o, Phosphate catalyzed exchange rates of NH-N protons of DNA. J. Biomol. Struct. Dyn. 6, 383-390 (1988).