NMR measurements of proton exchange between solvent and peptides and proteins

Acta Biochimica Polonica

Volumn 46, Issue 3, 1999, Pages 651-663

  Wójcik, Jacek ^a   Ruszczyńska, Katarzyna ^a   Zhukov, Igor ^a   Ejchart, Andrzej ^a  

^a INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

Author keywords

Magnetization transfer; NMR methods; Proton exchange

Indexed keywords

DEUTERIUM OXIDE; PEPTIDE; PROTEIN; PROTON; SOLVENT; WATER;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

AMINO ACID SEQUENCE; DEUTERIUM OXIDE; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEINS; PROTONS; SOLVENTS; WATER;

EID: 0033255139     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.1999_4137     Document Type: Article

References (47)

1. Englander, S.W. & Englander, J.J. (1978) Hydrogen - tritium exchange. Methods Enzymol. 49, 24-39.
2. Englander, S.W. & Kallenbach, N.R. (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16, 521-655.
3. 15N NMR spectroscopy: Use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein. Biochemistry 29, 6303-6313.
4. 1H NMR. Biochemistry 29, 5925-5934.
5. Sandström, J. (1982) Dynamic NMR Spectroscopy. Academic Press, London.
6. Lian, L.Y. & Roberts, G.C.K. (1993) NMR of Macromolecules. A Practical Approach (Roberts, G.C.K., ed.) pp. 153-182, Oxford University Press, Oxford.
7. Patel, D.J. & Canuel, L.L. (1976) Nuclear magnetic resonance studies of slowly exchanging peptide protons in cytochrome c in aqueous solution. Proc. Natl. Acad. Sci. U.S.A. 73, 1398-1402.
8. Wagner, G. & Wüthrich, K. (1982) Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. J. Mol. Biol. 160, 343-361.
9. 2. Biochemistry 29, 2278-2290.
10. 15N HMQC spectroscopy. Biochemistry 31, 443-450.
11. Ehrhardt, M.R., Urbauer, J.L. & Wand, A.J. (1995) The energetics and dynamics of molecular recognition by calmodulin. Biochemistry 34, 2731-2738.
12. Zhou, H.X., Hull, L.A., Kallenbach, N.R., Mayne, L., Bai, Y. & Englander, S.W. (1994) Quantitative evaluation of stabilizing interactions in a prenucleated a-helix by hydrogen exchange. J. Am. Chem. Soc. 116, 6482-6483.
13. Andrec, M., Hill, R.B. & Prestegard, J.H. (1995) Amide exchange rates in Escherichia coli acyl carrier protein: Correlation with protein structure and dynamics. Protein Sci. 4, 983-993.
14. Forsén, S. & Hoffman, R.A. (1963) Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance. J. Chem. Phys. 39, 2892-2901.
15. Frenkiel, T.A. (1993) NMR of Macromolecules. A Practical Approach (Roberts, G.C.K., ed.) pp. 35-70, Oxford University Press, Oxford.
16. Bloembergen, N. & Pound, R.V. (1954) Radiation damping in magnetic resonance experiments. Phys. Rev. 95, 8-12.
17. Altieri, A.S., Miller, K.E. & Byrd, R.A. (1996) A comparison of water suppression techniques using pulsed field gradients for high-resolution NMR of biomolecules. Magn. Reson. Rev. 17, 27-82.
18. McConnell, H.M. (1958) Reaction rates by nuclear magnetic resonace. J. Chem. Phys. 28, 430-431.
19. Ejchart, A., Siedlecka, M., Sticht, H. & Bierzyński, A. (1998) NMR studies of secondary structure in calcium binding hexadecapeptide. Bull Pol. Ac.: Chem. 46, 1-8.
20. Spera, S., Ikura, M. & Bax, A. (1991) Measurement of the exchange rates of rapidly exchanging amide protons: Application to the study of calmodulin and its complex with a myosin light chain kinase fragment. J. Biomol. NMR 1, 155-165.
21. Peng, J.W. & Wagner, G. (1992) Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments. Biochemistry 31, 8571-8586.
22. Zangger, K. & Sterk, H. (1995) NMR studies of exchanging amide protons in 1-desamino-8-D-argininevasopressin by selective Hartmann-Hahn transfer. Magn. Reson. Chem. 33, 124-127.
23. Redfield, A.G. & Waelder, S. (1979) Water solvent exchange rates of primary amides. Acid-catalyzed NMR saturation transfer as an indicator of rotation and structure of the protonated form. J. Am. Chem. Soc. 101, 6151-6162.
24. Rosevear, P.R., Fry, D.C. & Mildvan, A.S. (1985) Temperature dependence of the longitudinal relaxation rates and exchange rates of the amide protons in peptide substrates of protein kinase. J. Magn. Reson. 61, 102-115.
25. Henry, G.D. &Sykes, B.D. (1993) Saturation transfer of exchangeable protons in H-de-coupled : N INEPT spectra in water. Applica-tion to the measurement of hydrogen ex-change rates in amides and proteins. J. Magn. Reson. B102, 193-200.
26. Adams, B. & Lerner, L. (1992) A simple one-dimensional method for measuring proton exchange rates in water. J. Magn. Reson. A 96, 604-607.
27. Böckmann, A. & Guittet, E. (1996) Suppression of radiation damping during selective excitation of the water signal: The WANTED sequence. J. Biomol. NMR 8, 87-92.
28. Morris, G.A. & Freeman, R. (1978) Selective excitation in Fourier transform nuclear magnetic resonance. J. Magn. Reson. 29, 433-462.
29. Jeener, J., Meier, B.H., Bachman, P. & Ernst, R.R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
30. Schwartz, A.L. & Cutnell, J.D. (1983) One- and two-dimensional NMR studies of exchanging amide protons in glutathione. J. Magn. Reson. 53, 398-411.
31. Maudsley, A.A. & Ernst, R.R. (1977) Indirect detection of magnetic resonance by heteronuclear two-dimensional spectroscopy. Chem. Phys. Lett. 50, 368-372.
32. Bax, A., Griffey, R.H. & Hawkins, B.L. (1983) Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR. J. Magn. Reson. 55, 301-315.
33. Bodenhausen, G. & Reuben, D.J. (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69, 185-189.
34. Hore, P.J. (1989) Solvent suppression. Methods Enzymol. 176, 64-77.
35. Plateau, P. & Guéron, M. (1982) Exchangeable proton NMR without base-line distorsion, using new strong-pulse sequences. J. Am. Chem. Soc. 104, 7310-7311.
36. Piotto, M., Saudek, V. & Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
37. Ejchart, A. (1998) Application of field gradients in high resolution NMR. Bull. Pol. Ac.: Chem. 46, 117-131.
38. Abragam, A. (1989) Principles of Nuclear Magnetism. Chapter 8, Clarendon Press, Oxford.
39. Noggle, J.H. & Schirmer, R.E. (1971) The Nuclear Overhauser Effect. Chemical Applications Academic Press, New York, London.
40. Neuhaus, D. & Williamson, M.P. (1989) The Nuclear Overhauser Effect in Structural and Conformational Analysis. VCH Publishers, New York.
41. 2O. A method for measuring exchange and relaxation rates. J. Magn. Reson. 27, 455-463.
42. Campbell, I.D., Dobson, C.M., Ratcliffe, R.G. & Williams, R.J.P. (1978) Fourier transform NMR pulse methods for the measurements of slow-exchange rates. J. Magn. Reson. 29, 397-417.
43. Kriwacki, R.W., Hill, R.B., Flanagan, J.M., Caradonna, J.P. & Prestegard, J.H. (1993) New NMR methods for the characterization of bound waters in macromolecules. J. Am. Chem. Soc. 115, 8907-8911.
44. Gemmecker, G., Jahnke, W. & Kessler, H. (1993) Measurement of fast proton exchange rates in isotopically labeled compounds. J. Am. Chem. Soc. 115, 11620-11621.
45. Goch, G., Kozłowska, H., Wójtowicz, A. & Bierzyński, A. (1999) Acta Biochim. Polon. 46, 673-678.
46. Freeman, R. & Hill, H.D.W. (1971) Fourier transform study of NMR spin-lattice relaxation by "progressive saturation". J. Chem. Phys. 54, 3367-3377.
47. 15N relaxation parameters in proteins. Acta Biochim. Polon. 46, 665-672.