Assignment of 13C resonances and analysis of relaxation properties and internal dynamics of pike parvalbumin by 13C-NMR at natural abundance

European Journal of Biochemistry

Volumn 237, Issue 3, 1996, Pages 561-574

  Alattia, Temim ^a   Padilla, André ^a   Cavé, Adrien ^a,b  

^a CNRS   (France)

^b CENTRE DE BIOCHIMIE STRUCTURALE   (France)

Author keywords

13C NMR; Chemical shift; Molecular motion; Parvalbumin; Relaxation

Indexed keywords

PARVALBUMIN; CALCIUM; CARBON; HYDROGEN;

ARTICLE; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ESOCIDAE; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM; CARBON ISOTOPES; ESOCIDAE; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PARVALBUMINS; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

EID: 0029665215     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0561p.x     Document Type: Article

References (46)

1. Abragam, A. (1961) The principles of nuclear magnetism, Clarendon Press, Oxford.
2. Alexandrescu, A. T. & Shortle, D. (1994) Backbone dynamics of highly disordered 131 residue fragment of staphylococcal nuclease, J. Mol. Biol. 242, 527-546.
3. 13C-labelled α-carbon in motilin, J. Biomol. NMR 5, 133-146.
4. 2+ ions bound to proteins, J. Am. Chem. Soc. 104, 576-580.
5. Baldellon, C., Padilla, A. & Cavé, A. (1992) Kinetics of amide proton exchange in parvalbumin studied by 1H-2H 2-D NMR. A comparison of the calcium and magnesium loaded forms, Biochimie (Paris) 74, 837-844.
6. Bax, A., Griffey, R. H. & Hawkins, B. (1983) Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR, J. Magn. Reson, 55, 301-315.
7. Bendall, M. R., Pegg, D. T. & Doddrell, D. M. (1983) Pulse sequences utilizing the correlated motion of coupled heteronuclei in the transverse plane of the doubly rotating frame, J. Magn. Reson. 52, 81-117.
8. Braunschweiler, L. & Ernst, R. R. (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy, J. Magn. Reson. 53, 521-528.
9. Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C. & Gronenborn, A. M. (1990) J. Am. Chem. Soc. 112, 4989-4991.
10. de Dios, A. C., Pearson, J. G. & Oldfield, E. (1993) Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach, Science 260, 1491-1496.
11. 15N-enriched proteins, J. Biomol. NMR 5, 173-182.
12. Farrow, N. A., Zhang, O., Forman-Kay, J. D. & Kay, L. E. (1995a) Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer, Biochemistry 34, 868-878.
13. 15N relaxation data exclusively, J. Biomol. NMR 6, 153-162.
14. Fushman, D., Weisemann, R., Thüring, H. & Rüterjans, H. (1994) Backhone dynamics of ribonuclease T1 and its complex with 2′GMP studied by two-dimensional heteronuclear NMR spectroscopy, J. Biomol. NMR 4, 61-78.
15. 1H multiple quantum coherence spectroscopy, FEBS Lett. 243, 93-98.
16. 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease, Biochemistry 28, 8972-8979.
17. Kretsinger, R. H. & Nockolds, C. E. (1973) Carp muscle calcium-binding protein. II. Structure determination and general description, J. Biol. Chem. 248, 3313-3326.
18. β chemical shifts on protein structure determination by NMR, J. Magn. Reson. B 106, 92-96.
19. 13C resonances of apo-neocarzinostatine by two-dimensional heteronuclear NMR spectroscopy at natural abundance, J. Biomol. NMR 4, 689-702.
20. Lefèvre, J. F., Dayie, K. T., Peng, J. W. & Wagner, G. (1996) Internal mobility of the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density function, Biochemistry 35, 2674-2686.
21. Lerner, L. & Bax, A. (1986) Sensitivity-enhanced two-dimensional heteronuclear relayed coherence transfer NMR spectroscopy, J. Magn. Reson. 69, 375-380.
22. Lipari, G. & Szabo, A. (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, J. Am. Chem. Soc. 104, 4546-4559.
23. 1H spin-spin coupling constants in proteins, Biochem. Biophys. Res. Commun. 113, 967-974.
24. McCain, D. C., Ulrich, E. L. & Markley, J. L. (1988) NMR relaxation study of internal motions in staphylococcal nuclease, J. Magn. Reson. 80, 296-305.
25. 13C NMR methine relaxation at natural abundance, J. Biomol. NMR 5, 233-244.
26. 13C nuclear magnetic resonance study of molecular motions and conformational transitions in muscle calcium binding parvalbumins, Biochemistry 25, 5552-5560.
27. 1H nuclear magnetic resonance study of pike pI 5.0 parvalbumin (Esox lucius). Sequential resonance assignment and folding of the polypeptide chain, J. Mol. Biol. 204, 995-1017.
28. Padilla, A., Vuister, G. W., Boelens, R., Klewegt, G. J., Cavé, A., Parello, J. & Kaptein, R. (1990) Homonuclear three-dimensional proton NMR spectroscopy of pike parvalbumin. Comparison of short- and medium-range NOEs from two-dimensional and three-dimensional NMR, J. Am. Chem. Soc. 112, 5024.
29. 13C heteronuclear NMR spectroscopy, J. Am. Chem. Soc. 113, 4371-4380.
30. Parello, J., Cavé, A., Puigdomenech, P., Maury, C., Capony, J. P. & Pechère, J. F. (1974) Conformational studies on muscular parvalbumins. II. Nuclear magnetic resonance analysis, Biochimie (Paris) 56, 61.
31. Pastore, A. & Saudek, V. (1990) The relationship between chemical shift and secondary structure in proteins, J. Magn. Reson. 90, 165-176.
32. Pechère, J.-F., Demaille, J. & Capony, J.-P. (1971) Muscular parvalbumins: preparative and analytical method of general applicability, Biochim. Biophys. Acta 236, 391-408.
33. Peng, J. W. & Wagner, G. (1992a) Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments, Biochemistry 31, 8571-8586.
34. Peng, J. W. & Wagner, G. (1992b) Mapping of spectral density functions using heteronuclear NMR relaxation measurements, J. Magn. Reson. 98, 308-332.
35. Peng, J. W. & Wagner, G. (1994) Protein motions via relaxation experiments, Methods Enzymol. 239, 563-596.
36. Press, W. H., Flannery, B. P., Teukolsky, S. A. & Vetterling, W. T. (1986) Numerical Recipes, Cambridge University Press, Cambridge.
37. Rance, M., Sørensen, O. W., Bodenhausen, G., Wagner, G., Ernst, R. R. & Wüthrich, K. (1983) Biochem. Biophys. Res. Commun. 117, 479-485.
38. Shaka, A. J., Keeler, J., Frenkiel, T. & Freeman, R. (1983) An improved sequence for broadband decoupling: WALTZ-16, J. Magn. Reson. 52, 335-338.
39. Shaka, A. J., Barker, P. B. & Freeman, R. (1985) Computer-optimised decoupling scheme for wideband applications and low-level operation, J. Magn. Reson. 64, 547-552.
40. 15N spin relaxation measurements, J. Magn. Reson. B 102, 253-264.
41. 13C nuclear magnetic resonance chemical shifts, J. Am. Chem. Soc. 113, 5490-5492.
42. Strydnaka, N. C. J. & James, M. N. G. (1989) Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58, 951-998.
43. 2 -binding protein parvalbumin, Eur. J. Biochem. 230, 498-502.
44. Williams, R. J. P. (1989) NMR studies of mobility within protein structure, Eur. J. Biochem. 183, 479-497.
45. Wishart, D. S. & Sykes, B. D. (1994a) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data, J. Biomol. NMR 4, 171-180.
46. Wishart, D. S. & Sykes, B. D. (1994b) Chemical shifts as a tool for structural determination, Methods Enzymol. 239, 363-392.