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. 1995 Sep 26;92(20):9279–9283. doi: 10.1073/pnas.92.20.9279

Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.

J R Tolman 1, J M Flanagan 1, M A Kennedy 1, J H Prestegard 1
PMCID: PMC40968  PMID: 7568117

Abstract

The measurement of dipolar contributions to the splitting of 15N resonances of 1H-15N amide pairs in multidimensional high-field NMR spectra of field-oriented cyanometmyoglobin is reported. The splittings appear as small field-dependent perturbations of normal scalar couplings. Assignment of more than 90 resonances to specific sequential sites in the protein allows correlation of the dipolar contributions with predictions based on the known susceptibility and known structure of the protein. Implications as an additional source of information for protein structure determination in solution are discussed.

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Selected References

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  1. Banci L., Bertini I., Luchinat C. Two-dimensional nuclear magnetic resonance spectra of paramagnetic systems. Methods Enzymol. 1994;239:485–514. doi: 10.1016/s0076-6879(94)39019-3. [DOI] [PubMed] [Google Scholar]
  2. Cheng X. D., Schoenborn B. P. Neutron diffraction study of carbonmonoxymyoglobin. J Mol Biol. 1991 Jul 20;220(2):381–399. doi: 10.1016/0022-2836(91)90020-7. [DOI] [PubMed] [Google Scholar]
  3. Edison A. S., Abildgaard F., Westler W. M., Mooberry E. S., Markley J. L. Practical introduction to theory and implementation of multinuclear, multidimensional nuclear magnetic resonance experiments. Methods Enzymol. 1994;239:3–79. doi: 10.1016/s0076-6879(94)39003-7. [DOI] [PubMed] [Google Scholar]
  4. Emerson S. D., La Mar G. N. NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin: a new probe of steric tilt of bound ligand. Biochemistry. 1990 Feb 13;29(6):1556–1566. doi: 10.1021/bi00458a029. [DOI] [PubMed] [Google Scholar]
  5. Emerson S. D., La Mar G. Solution structural characteristics of cyanometmyoglobin: resonance assignment of heme cavity residues by two-dimensional NMR. Biochemistry. 1990 Feb 13;29(6):1545–1556. doi: 10.1021/bi00458a028. [DOI] [PubMed] [Google Scholar]
  6. Horrocks W. D., Jr, Greenberg E. S. Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems: ferricytochrome c and metmyoglobin cyanide. Biochim Biophys Acta. 1973 Sep 21;322(1):38–44. doi: 10.1016/0005-2795(73)90172-4. [DOI] [PubMed] [Google Scholar]
  7. Lecomte J. T., Johnson R. D., La Mar G. N. Characterization of heme orientational disorder in myoglobin by proton nuclear Overhauser effects. Biochim Biophys Acta. 1985 Jun 10;829(2):268–274. doi: 10.1016/0167-4838(85)90197-9. [DOI] [PubMed] [Google Scholar]
  8. Neidhardt F. C., Bloch P. L., Smith D. F. Culture medium for enterobacteria. J Bacteriol. 1974 Sep;119(3):736–747. doi: 10.1128/jb.119.3.736-747.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Thériault Y., Pochapsky T. C., Dalvit C., Chiu M. L., Sligar S. G., Wright P. E. 1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin. J Biomol NMR. 1994 Jul;4(4):491–504. doi: 10.1007/BF00156616. [DOI] [PubMed] [Google Scholar]
  10. Wüthrich K., Wider G., Wagner G., Braun W. Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance. J Mol Biol. 1982 Mar 5;155(3):311–319. doi: 10.1016/0022-2836(82)90007-9. [DOI] [PubMed] [Google Scholar]

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