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

J. R. Tolman, J. M. Flanagan, M. A. Kennedy, J. H. Prestegard

Research output: Contribution to journalArticlepeer-review

721 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)9279-9283
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number20
DOIs
StatePublished - Sep 26 1995

All Science Journal Classification (ASJC) codes

  • General

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