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

by: JR Tolman, JM Flanagan, MA Kennedy, JH Prestegard

Proc Natl Acad Sci U S A, Vol. 92, No. 20. (26 September 1995), pp. 9279-9283.

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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.

@article{citeulike:1370462, 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.}, address = {Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA.}, author = {Tolman, J. R. and Flanagan, J. M. and Kennedy, M. A. and Prestegard, J. H. }, citeulike-article-id = {1370462}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {nmr, rdc}, month = {September}, number = {20}, pages = {9279--9283}, posted-at = {2007-06-07 15:18:13}, priority = {2}, title = {Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/7568117}, volume = {92}, year = {1995} }

RIS record

TY - JOUR ID - citeulike:1370462 L3 - citeulike-article-id:1370462 N2 - 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. IS - 20 JF - Proc Natl Acad Sci U S A SN - 0027-8424 AD - Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA. EP - 9283 TI - Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution. VL - 92 SP - 9279 KW - nmr KW - rdc AU - Tolman, JR AU - Flanagan, JM AU - Kennedy, MA AU - Prestegard, JH PY - 1995/09/26/ UR - http://view.ncbi.nlm.nih.gov/pubmed/7568117 ER -

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