A set of 4D NMR experiments of enhanced resolution for easy resonance assignment in proteins

Journal of Magnetic Resonance

Volumn 202, Issue 1, 2010, Pages 109-116

  Zawadzka Kazimierczuk, Anna ^a   Kazimierczuk, Krzysztof ^a   Koźmiński, Wiktor ^a  

^a UNIVERSITY OF WARSAW   (Poland)

Author keywords

CsPin; Maltose binding protein; NMR; Proteins; Random sampling; Resonance assignment; Sparse multidimensional Fourier transform

Indexed keywords

CSPIN; MALTOSE BINDING PROTEINS; MULTIDIMENSIONAL FOURIER TRANSFORM; RANDOM SAMPLING; RESONANCE ASSIGNMENTS;

FOURIER TRANSFORMS; MALTOSE; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RESONANCE; SEMICONDUCTOR QUANTUM DOTS;

PROTEINS;

PROTEIN;

ALGORITHM; ARTICLE; CHEMISTRY; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE MAPPING;

ALGORITHMS; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE MAPPING; PROTEINS;

EID: 72149090106     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2009.10.006     Document Type: Article

References (27)

1. Wüthrich K. NMR of Proteins and Nucleic Acids (1986), Wiley-Interscience, New York
2. Cavanagh J., Fairbrother W.J., Palmer III A.G., Skelton N.J., and Rance M. Protein NMR Spectroscopy: Principles and Practice. second ed. (2007), Academic Press, Boston
3. Cornilescu G., Marquardt J.L., Ottiger M., and Bax A. Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J. Am. Chem. Soc. 120 (1998) 6836-6837
4. Karplus M. Vicinal proton coupling in nuclear magnetic resonance. J. Am. Chem. Soc. 85 (1963) 2870-2871
5. Tjandra N., and Bax A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278 (1997) 1111-1114
6. Ikura M., Kay L.E., and Bax A. A novel approach for sequential assignment of 1H, C-13, and N-15 spectra of larger proteins: heteronuclear triple resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry 29 (1990) 4659-4667
7. Moseley H.N.B., and Montelione G.T. Automated analysis of NMR assignments and structures for proteins. Curr. Opin. Struct. Biol. 9 (1999) 635
8. Szantay C. NMR and the uncertainty principle: How to and how not to interpret homogeneous line broadening and pulse nonselectivity. III. Uncertainty?. Concepts Magn. Reson. A 32A (2008) 302-325
9. Kazimierczuk K., Zawadzka A., Koźmiński W., and Zhukov I. Random sampling of evolution time space and Fourier transform processing. J. Biomol. NMR 36 (2006) 157-168
10. Rovnyak D., Frueh D.P., Sastry M., Sun Z.Y.J., Stern A.S., Hoch J.C., and Wagner G. Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction. J. Magn. Reson. 170 (2004) 15-21
11. Stern A.S., and Hoch J.C. Maximum entropy reconstruction in NMR. In: Grant D.M., and Harris R. (Eds). Encyclopedia of Nuclear Magnetic Resonance vol. 8 (1996), John Wiley & Sons, Chichester, UK
12. Tugarinov V., Kay L.E., Ibraghimov I., and Orekhov V.Y. High-resolution four-dimensional H-1-C-13 NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition. J. Am. Chem. Soc. 127 (2005) 2767-2775
13. Zhang F.L., and Bruschweiler R. Indirect covariance NMR spectroscopy. J. Am. Chem. Soc. 126 (2004) 13180-13181
14. Bilinskis I. Digital Alias-free Signal Processing (2007), Wiley
15. Kazimierczuk K., Zawadzka A., Koźmiński W., and Zhukov I. Determination of spin-spin couplings from ultra-high resolution 3D NMR spectra obtained by optimized random sampling and multidimensional Fourier transformation. J. Am. Chem. Soc. 130 (2008) 5404-5405
16. Kazimierczuk K., Zawadzka A., and Koźmiński W. Narrow peaks and high dimensionalities: exploiting the advantages of random sampling. J. Magn. Reson. 197 (2009) 219-228
17. 15N enriched proteins. J. Biomol. NMR 1 (1991) 99-104
18. 13C labeled proteins. J. Magn. Reson. 97 (1992) 213-217
19. Wittekind M., and Mueller L. HNCACB: a high-sensitivity 3D NMR experiment to correlate amide proton and nitrogen resonances with the alpha-carbon and beta-carbon resonances in proteins. J. Magn. Reson. B101 (1993) 201-205
20. Grzesiek S., and Bax A. An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J. Magn. Reson. 99 (1992) 201-207
21. 13C-labelled proteins. J. Biomol. NMR 3 (1993) 113-120
22. Kazimierczuk K., Zawadzka A., and Koźmiński W. Optimization of random time domain sampling in multidimensional NMR. J. Magn. Reson. 192 (2008) 123-130
23. Coggins B.E., Venters R.A., and Zhou P. Generalized reconstruction of n-D NMR spectra from multiple projections: application to the 5-D HACACONH spectrum of protein G B1 domain. J. Am. Chem. Soc. 126 (2004) 1000-1001
24. Coggins B.E., and Zhou P. PR-CALC: a program for the reconstruction of NMR spectra from projections. J. Biomol. NMR 34 (2006) 179-195
25. T.D. Goddard, D.G. Kneller, SPARKY 3, University of California, San Francisco.
26. Pervushin K., Riek R., Wider G., and Wüthrich K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. USA 94 (1997) 12366-12371
27. Schanda P., Kupce E., and Brutscher B. SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J. Biomol. NMR 33 (2005) 199-211