Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1992 Sep 25;20(18):4747–4751. doi: 10.1093/nar/20.18.4747

Heteronuclear NMR of DNA with the heteronucleus in natural abundance: facilitated assignment and extraction of coupling constants.

P Schmieder 1, J H Ippel 1, H van den Elst 1, G A van der Marel 1, J H van Boom 1, C Altona 1, H Kessler 1
PMCID: PMC334227  PMID: 1408787

Abstract

Two heteronuclear proton-carbon NMR experiments are applied to the DNA-octamer d(TTGGCCAA)2 with carbon in natural abundance. They lead to a complete assignment of the carbon resonances of the sugars and bases. In addition, several heteronuclear coupling constants, proton-carbon as well as proton-phosphorous and phosphorous-carbon, were determined. The information can be obtained in a reasonable measuring time and offers valuable information for a detailed picture of DNA structure.

Full text

PDF
4747

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ashcroft J., Live D. H., Patel D. J., Cowburn D. Heteronuclear two-dimensional 15N- and 13C-NMR studies of DNA oligomers and their netropsin complexes using indirect proton detection. Biopolymers. 1991 Jan;31(1):45–55. doi: 10.1002/bip.360310105. [DOI] [PubMed] [Google Scholar]
  2. Bax A., Sparks S. W., Torchia D. A. Detection of insensitive nuclei. Methods Enzymol. 1989;176:134–150. doi: 10.1016/0076-6879(89)76009-2. [DOI] [PubMed] [Google Scholar]
  3. Fesik S. W., Zuiderweg E. R. Heteronuclear three-dimensional NMR spectroscopy of isotopically labelled biological macromolecules. Q Rev Biophys. 1990 May;23(2):97–131. doi: 10.1017/s0033583500005515. [DOI] [PubMed] [Google Scholar]
  4. Ikura M., Kay L. E., Bax A. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry. 1990 May 15;29(19):4659–4667. doi: 10.1021/bi00471a022. [DOI] [PubMed] [Google Scholar]
  5. LaPlante S. R., Ashcroft J., Cowburn D., Levy G. C., Borer P. N. 13C NMR assignments of the protonated carbons of [d(TAGCGCTA)]2 by two-dimensional proton-detected heteronuclear correlation. J Biomol Struct Dyn. 1988 Apr;5(5):1089–1099. doi: 10.1080/07391102.1988.10506450. [DOI] [PubMed] [Google Scholar]
  6. LaPlante S. R., Boudreau E. A., Zanatta N., Levy G. C., Borer P. N., Ashcroft J., Cowburn D. 13C NMR of the bases of three DNA oligonucleotide duplexes: assignment methods and structural features. Biochemistry. 1988 Oct 4;27(20):7902–7909. doi: 10.1021/bi00420a048. [DOI] [PubMed] [Google Scholar]
  7. Lankhorst P. P., Erkelens C., Haasnoot C. A., Altona C. Carbon-13 NMR in conformational analysis of nucleic acid fragments. Heteronuclear chemical shift correlation spectroscopy of RNA constituents. Nucleic Acids Res. 1983 Oct 25;11(20):7215–7230. doi: 10.1093/nar/11.20.7215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Leupin W., Wagner G., Denny W. A., Wüthrich K. Assignment of the 13C nuclear magnetic resonance spectrum of a short DNA-duplex with 1H-detected two-dimensional heteronuclear correlation spectroscopy. Nucleic Acids Res. 1987 Jan 12;15(1):267–275. doi: 10.1093/nar/15.1.267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. McIntosh L. P., Dahlquist F. W. Biosynthetic incorporation of 15N and 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins. Q Rev Biophys. 1990 Feb;23(1):1–38. doi: 10.1017/s0033583500005400. [DOI] [PubMed] [Google Scholar]
  10. Nikonowicz E. P., Pardi A. Three-dimensional heteronuclear NMR studies of RNA. Nature. 1992 Jan 9;355(6356):184–186. doi: 10.1038/355184a0. [DOI] [PubMed] [Google Scholar]
  11. Santos R. A., Tang P., Harbison G. S. Determination of the DNA sugar pucker using 13C NMR spectroscopy. Biochemistry. 1989 Nov 28;28(24):9372–9378. doi: 10.1021/bi00450a018. [DOI] [PubMed] [Google Scholar]
  12. Schmieder P., Kurz M., Kessler H. Determination of heteronuclear long-range couplings to heteronuclei in natural abundance by two- and three-dimensional NMR spectroscopy. J Biomol NMR. 1991 Nov;1(4):403–420. doi: 10.1007/BF02192863. [DOI] [PubMed] [Google Scholar]
  13. Stockman B. J., Reily M. D., Westler W. M., Ulrich E. L., Markley J. L. Concerted two-dimensional NMR approaches to hydrogen-1, carbon-13, and nitrogen-15 resonance assignments in proteins. Biochemistry. 1989 Jan 10;28(1):230–236. doi: 10.1021/bi00427a032. [DOI] [PubMed] [Google Scholar]
  14. Wagner G. Heteronuclear nuclear magnetic resonance experiments for studies of protein conformation. Methods Enzymol. 1989;176:93–113. doi: 10.1016/0076-6879(89)76007-9. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES