Use of deuterium labeling in NMR: Overcoming a sizeable problem

Structure

Volumn 4, Issue 11, 1996, Pages 1245-1249

  Sattler, Michael ^a   Fesik, Stephen W ^a  

^a ABBOTT LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0030589110     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00133-5     Document Type: Article

References (32)

1. Clore, G.M. & Gronenborn, A.M. (1994). Multidimensional heteronuclear nuclear magnetic resonance of proteins. Methods Enzymol. 239, 349-363.
2. LeMaster, D.M. & Richards, F.M. (1988). NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation. Biochemistry 27, 142-150.
3. Torchia, D.A., Sparks, S.W. & Bax, A. (1988). Delineation of α-helical domains in deuteriated staphylococcal nuclease by 2D NOE NMR spectroscopy. J. Am. Chem. Soc. 110, 2320-2321.
4. 13C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins. J. Am. Chem. Soc. 95, 1316-1323.
5. 15N-enriched proteins. Application to triple resonance 4D J connectivity of sequential amides. J. Am. Chem. Soc. 115, 4369-4370.
6. 2H enrichment and decoupling. J. Biomol. NMR 3, 701-708.
7. 2H-labeled proteins: application to a 37-kDa trp repressor-DNA complex. J. Am. Chem. Soc. 116, 6464-6465.
8. LeMaster, D.M. (1994). Isotope labeling in solution protein assignment and structural analysis. Prog. NMR Spectrosc. 26, 371-419.
9. 1H-leucine side chains. Science 161, 795-796.
10. Markley, J.L., Putter, I. & Jardetzky, O. (1968). High-resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease. Science 161, 1249-1251.
11. Tsang, P., Wright, P.E. & Rance, M. (1990). Specific deuteration strategy for enhancing direct nuclear Overhauser effects in high molecular weight complexes. J. Am. Chem. Soc. 112, 8183-8185.
12. 1H NMR NOESY spectra of a large protein by selective deuteriation. J. Am. Chem. Soc. 113, 2787-2789.
13. 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor. Biochemistry 29, 6332-6341.
14. 15N-labeled protein: potential in structure determination of large proteins by NMR. J. Am. Chem. Soc. 118, 6800-6801.
15. Shon, K.-J., Kim, Y., Colnago, L.A. & Opella, S.J. (1991). NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein. Science 252, 1303-1305.
16. 1H-NMR spectroscopy on elongation factor Tu from Escherichia coli. FEBS Lett. 180, 40-42.
17. 2H labeled proteins with high sensitivity. J. Am. Chem. Soc. 116, 11655-11666.
18. 15N labeling of proteins for NMR studies. J. Biomol. NMR 5, 339-344.
19. Kay, L.E., Ikura, M., Tschudin, R. & Bax, A. (1990). Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89, 496-514.
20. Zhou, M.-M., et al., & Fesik, S.W. (1995). Structure and ligand recognition of the phosphotyrosine binding domain of She. Nature 378, 584-592.
21. 2H-decoupling. J. Am. Chem. Soc. 118, 6570-6579.
22. Nietlispach, D., et al., & Laue, E.D. (1996). An approach to the structure determination of larger proteins using triple resonance NMR experiments in conjunction with random fractional deuteration. J. Am. Chem. Soc. 118, 407-415.
23. 13C magnetization transfer via isotropic mixing. Spin system identification in large proteins. J. Am. Chem. Soc. 112, 886-888.
24. 13C-enriched proteins. J. Magn. Reson. 88, 425-431.
25. Logan, T.M., Olejniczak, E.T., Xu, R.X. & Fesik, S.W. (1992). Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments. FEBS Lett. 314, 413-418.
26. Montelione, G.T., Lyons, B.A, Emerson, S.D. & Tashiro, M. (1992). An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins. J. Am. Chem. Soc. 114, 10974-10975.
27. 13C magnetization. J. Magn. Reson. B 101, 114-119.
28. 13C resonances in perdeuterated proteins. J. Am. Chem. Soc. 117, 4187-4188.
29. 15N-enriched proteins. Application to HIV-1 Nef. J. Am. Chem. Soc. 117, 9594-9595.
30. N NOEs to determine protein global folds in perdeuterated proteins. J. Am. Chem. Soc. 117, 9592-9593.
31. L, an inhibitor of programmed cell death. Nature 381, 335-341.
32. L-Bak peptide complex reveals how regulators of apoptosis interact. Science, in press.