Z κ: AA transverse relaxation optimized spectroscopy NMR experiment measuring longitudinal relaxation interference

Journal of Chemical Physics

Volumn 128, Issue 15, 2008, Pages

  Weaver, Daniel S ^a   Zuiderweg, Erik R P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; BIOMOLECULES; CHEMICAL SHIFT; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTONATION;

BIOMOLECULAR ROTATIONAL DYNAMICS; BIOSYSTEMS; HUMAN UBIQUITIN; SUBNANOSECOND TIME SCALES;

PEPTIDES;

PROTEIN;

ALGORITHM; ARTICLE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ULTRASTRUCTURE;

ALGORITHMS; COMPUTER SIMULATION; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEINS;

EID: 42449149199     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.2889923     Document Type: Article

References (35)

1. M. Karplus and J. Kuriyan, Proc. Natl. Acad. Sci. U.S.A. 102, 6679 (2005).
2. P. Maragakis and M. Karplus, J. Mol. Biol. 352, 807 (2005).
3. J. A. Hoerter, M. N. Lambert, M. J. Pereira, and N. G. Walter, Biochemistry 43, 14624 (2004).
4. W. Min, B. P. English, G. Luo, B. J. Cherayil, S. C. Kou, and X. S. Xie, Acc. Chem. Res. 38, 923 (2005).
5. D. Bourgeois, B. Vallone, A. Arcovito, G. Sciara, F. Schotte, P. A. Anfinrud, and M. Brunori, Proc. Natl. Acad. Sci. U.S.A. 103, 4924 (2006).
6. Q. Xu, H. Guo, A. Wlodawer, and H. Guo, J. Am. Chem. Soc. 128, 5994 (2006).
7. H. J. Dyson and P. E. Wright, Nat. Rev. Mol. Cell Biol. 6, 197 (2005).
8. L. E. Kay, D. A. Torchia, and A. Bax, Biochemistry 28, 8972 (1989).
9. A. Mittermaier and L. E. Kay, Science 312, 224 (2006).
10. T. Wang, K. K. Frederick, T. I. Igumenova, A. J. Wand, and E. R. P. Zuiderweg, J. Am. Chem. Soc. 127, 828 (2005).
11. U. Brath, M. Akke, D. Yang, L. E. Kay, and F. A. A. Mulder, J. Am. Chem. Soc. 128, 5718 (2006).
12. R. B. Best, J. Clarke, and M. Karplus, J. Mol. Biol. 349, 185 (2005).
13. L. Wang, Y. Pang, T. Holder, J. R. Brender, A. Kurochkin, and E. R. P. Zuiderweg, Proc. Natl. Acad. Sci. U.S.A. 98, 7684 (2001).
14. E. Z. Eisenmesser, O. Millet, W. Labeikovsky, D. M. Korzhnev, M. Wolf-Watz, D. A. Bosco, J. J. Skalicky, L. E. Kay, and D. Kern, Nature (London) 438, 117 (2005).
15. Q. Zhang, X. Sun, E. D. Watt, and H. M. Al-Hashimi, Science 311, 653 (2006).
16. M. W. F. Fischer, A. Majumdar, and E. R. P. Zuiderweg, Prog. Nucl. Magn. Reson. Spectrosc. 33, 207 (1994).
17. C. D. Kroenke, J. P. Loria, L. K. Lee, M. Rance, and A. G. Palmer III, J. Am. Chem. Soc. 120, 7905 (1998).
18. L. Wang, A. V. Kurochkin, and E. R. P. Zuiderweg, J. Magn. Reson. 144, 175 (2000).
19. I. C. Felli, H. Desvaux, and G. Bodenhausen, J. Biomol. NMR 12, 509 (1998).
20. S. Bouguet-Bonnet, P. Mutzenhardt, and D. Canet, J. Biomol. NMR 30, 133 (2004).
21. P. Pelupessy, F. Ferrage, and G. Bodenhausen, J. Chem. Phys. 126, 134508 (2007).
22. K. Pervushin, R. Riek, G. Wider, and K. Wüthrich, Proc. Natl. Acad. Sci. U.S.A. 94, 12366 (1997).
23. T. I. Igumenova and A. G. Palmer III, J. Am. Chem. Soc. 0002-7863 10.1021/ja061692f 128, 8110 (2006); T. I. Igumenova and A. G. Palmer III, J. Am. Chem. Soc. 128, 8110 (2006).
24. Q. Gong and R. Ishima, J. Biomol. NMR 37, 147 (2007).
25. M. Goldman, Quantum Description of High-Resolution NMR in Liquids (Oxford University Press, Oxford, 1991).
26. F. Ferrage, P. Pelupessy, D. Cowburn, and G. Bodenhausen, J. Am. Chem. Soc. 128, 11072 (2006).
27. T. Schulte-Herbrüggen and O. W. Sørensen, J. Magn. Reson. 144, 123 (2000).
28. F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer, and A. Bax, J. Biomol. NMR 6, 277 (1995).
29. T. D. Goddard and G. D. Kneller, SPARKY 3, University of California, San Francisco.
30. See EPAPS Document No. E-JCPSA6-128-012812 for one table with fitted rates for ubiquitin, extracted from the experiments, and for two tables with fitted rates for smMLCKp-complexed calcium-saturated chicken calmodulin, extracted from the experiments, at different spectrometer field strengths. This document can be reached through a direct link in the online article's HTML reference section or via the EPAPS homepage (http://www.aip.org/pubservs/epaps. html).
31. G. Lipari and A. Szabo, J. Am. Chem. Soc. 104, 4546 (1982).
32. L. E. Kay, P. Keifer, and T. Saarinen, J. Am. Chem. Soc. 114, 10663 (1992).
33. M. Rance, J. P. Loria, and A. G. Palmer III, J. Magn. Reson. 136, 92 (1999).
34. M. H. A. Roerhl, G. J. Heffron, and G. Wagner, J. Magn. Reson. 174, 325 (2005).
35. A. L. Lee, S. A. Kinnear, and A. J. Wand, Nat. Struct. Biol. 7, 72 (2000).