13C direct-detection biomolecular NMR spectroscopy in living cells

Angewandte Chemie - International Edition

Volumn 50, Issue 10, 2011, Pages 2339-2341

  Bertini, Ivano ^a   Felli, Isabella C ^a   Gonnelli, Leonardo ^a   Vasantha Kumar, M V ^a   Pierattelli, Roberta ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Biological cells; Biomolecules; Isotopic labeling; NMR spectroscopy; Proteins

Indexed keywords

[CARBONYL; BIO-MOLECULAR; BIOLOGICAL CELLS; DIRECT RESPONSE; DIRECT-DETECTION; E. COLI; FOLDED PROTEINS; HETERONUCLEAR; ISOTOPIC LABELING; LIVING CELL; NMR SPECTROSCOPY; PROTEIN FRAGMENTS; UNFOLDED PROTEINS;

BIOMOLECULES; CELLS; ESCHERICHIA COLI; ISOTOPES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

PROTEINS;

ALPHA SYNUCLEIN; ATX1 PROTEIN, S CEREVISIAE; CARBON; CARRIER PROTEIN; CATION TRANSPORT PROTEIN; CHAPERONE; COX17 PROTEIN, S CEREVISIAE; ESCHERICHIA COLI PROTEIN; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; CHEMISTRY; ESCHERICHIA COLI; GENETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN UNFOLDING; SACCHAROMYCES CEREVISIAE;

ALPHA-SYNUCLEIN; CARBON ISOTOPES; CARRIER PROTEINS; CATION TRANSPORT PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MOLECULAR CHAPERONES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN UNFOLDING; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 79952045339     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201006636     Document Type: Article

References (34)

1. Z. Serber, A. T. Keatinge-Clay, R. Ledwidge, A. E. Kelly, S. M. Miller, V. Dötsch, J. Am. Chem. Soc. 2001, 123, 2446-2447.
2. M. M. Dedmon, C. N. Patel, G. B. Young, G. J. Pielak, Proc. Natl. Acad. Sci. USA 2002, 99, 12681-12684.
3. Z. Serber, P. Selenko, R. Haensel, S. Reckerl, F. Loehr, J. E. Ferrel, G. Wagner, V. Dötsch, Nat. Protoc. 2007, 1, 2701-2709.
4. P. Selenko, G. Wagner, J. Struct. Biol. 2007, 158, 244-253.
5. G. Lippens, I. Landrieu, X. Hanoulle, Chem. Biol. 2008, 15, 311-312.
6. G. J. Pielak, C. Li, A. C. Miklos, A. P. Schlesinger, K. M. Slade, G. F. Wang, I. G. Zigoneanu, Biochemistry 2009, 48, 226-234.
7. D. Sakakibara, A. Sasaki, T. Ikeya, J. Hamatsu, T. Hanashima, M. Mishima, M. Yoshimasu, N. Hayashi, T. Mikawa, M. Waelchili, B. O. Smith, M. Shirakawa, P. Guentert, Y. Ito, Nature 2009, 458, 102-105.
8. Z. Serber, R. Ledwidge, S. M. Miller, V. Dötsch, J. Am. Chem. Soc. 2001, 123, 8895-8901.
9. P. Selenko, Z. Serber, B. Gadea, J. Ruderman, G. Wagner, Proc. Natl. Acad. Sci. USA 2006, 103, 11904-11909.
10. T. Sakai, H. Tochio, T. Tenno, Y. Ito, T. Kokubo, H. Hiroaki, M. Shirakawa, J. Biomol. NMR 2006, 36, 179-188.
11. J. F. Bodart, J. M. Wieruszeski, L. Amniai, A. Leroy, I. Landrieu, A. Rousseau-Lescuyer, J. P. Vilain, G. Lippens, J. Magn. Reson. 2008, 192, 252-257.
12. K. Inomata, A. Ohno, H. Tochio, S. Isogai, T. Tenno, I. Nakase, T. Takeuchi, S. Futaki, Y. Ito, H. Hirokai, M. Shirakawa, Nature 2009, 458, 106-109.
13. D. S. Burz, K. Dutta, D. Cowburn, A. Shekhtman, Nat. Methods 2006, 3, 91-93.
14. S. Reckel, R. Hänsel, F. Löhr, V. Dötsch, Prog. Nucl. Magn. Reson. Spectrosc. 2007, 51, 91-101.
15. P. Selenko, D. P. Frueh, S. J. Elsaesser, W. Haas, S. P. Gygi, G. Wagner, Nat. Struct. Mol. Biol. 2008, 15, 321-329.
16. P. N. Reardon, L. D. Spicer, J. Am. Chem. Soc. 2005, 127, 10848-10849.
17. N. Shimba, Z. Serber, R. Ledwidge, S. M. Miller, C. S. Craik, V. Dötsch, Biochemistry 2003, 42, 9227-9234.
18. Z. Serber, W. Straub, L. Corsini, A. M. Nomura, N. Shimba, C. S. Craik, P. R. Ortiz de Montellano, V. Dötsch, J. Am. Chem. Soc. 2004, 126, 7119-7125.
19. W. Bermel, I. Bertini, I. C. Felli, M. Piccioli, R. Pierattelli, Prog. Nucl. Magn. Reson. Spectrosc. 2006, 48, 25-45.
20. W. Bermel, I. Bertini, I. C. Felli, R. Pierattelli, J. Am. Chem. Soc. 2009, 131, 15339-15345.
21. F. Arnesano, E. Balatri, L. Banci, I. Bertini, D. R. Winge, Structure 2005, 13, 713-722.
22. F. Arnesano, L. Banci, I. Bertini, D. L. Huffman, T. V. O'Halloran, Biochemistry 2001, 40, 1528-1539.
23. R. L. Croke, C. O. Sallum, E. Watson, E. D. Watt, A. T. Alexandrescu, Protein Sci. 2008, 17, 1434-1445.
24. P. Schanda, B. Brutscher, J. Am. Chem. Soc. 2005, 127, 8014-8015.
25. W. Bermel, I. Bertini, I. C. Felli, R. Kümmerle, R. Pierattelli, J. Magn. Reson. 2006, 178, 56-64.
26. W. Bermel, I. Bertini, L. Duma, L. Emsley, I. C. Felli, R. Pierattelli, P. R. Vasos, Angew. Chem. 2005, 117, 3149-3152;
27. Angew. Chem. Int. Ed. 2005, 44, 3089-3092.
28. W. Bermel, I. Bertini, V. Csizmok, I. C. Felli, R. Pierattelli, P. Tompa, J. Magn. Reson. 2009, 198, 275-281.
29. C. Li, G. F. Wang, Y. Wang, R. Creager-Allen, E. A. Lutz, H. Scronce, K. M. Slade, R. A. Ruf, R. A. Mehl, G. J. Pielak, J. Am. Chem. Soc. 2010, 132, 321-327.
30. W. Bermel, I. Bertini, I. C. Felli, Y.-M. Lee, C. Luchinat, R. Pierattelli, J. Am. Chem. Soc. 2006, 128, 3918-3919.
31. C. Li, L. M. Charlton, A. Lakkavaram, C. Seagle, G. Wang, G. B. Young, J. M. Macdonald, G. J. Pielak, J. Am. Chem. Soc. 2008, 130, 6310-6311.
32. I. Bertini, I. C. Felli, L. Gonnelli, R. Pierattelli, Z. Spyranti, G. A. Spyroulias, J. Biomol. NMR 2006, 36, 111-122.
33. C. Li, Y. Wang, G. J. Pielak, J. Phys. Chem. B 2009, 113, 13390-13392.
34. It should be remembered that with increasing effective correlation times the large carbonyl chemical shift anisotropy and the long coherence transfer delays in CON experiments cause significant sensitivity losses, which are generally larger than those affecting H-N correlation experiments.