caa a22 4500 477136478 CHVBK 20180405111719.0 cr unu---uuuuu 170330e19970601xx s 000 0 eng 10.1023/A:1018342425634 doi (NATIONALLICENCE)springer-10.1023/A:1018342425634 Unambiguous NOE assignments in proteins by a combination of through-bond and through-space correlations [Elektronische Daten] [Frank Löhr, Heinz Rüterjans] Heteronuclear editing has found widespread use in the detection ofproton-proton dipolar interactions in isotopically labelled proteins.However, in cases where both the resonances of protons and directly bound13C or 15N spins of two or more sites aredegenerate, unambiguous assignments are difficult to obtain by conventionalmethods. Here, we present simple extensions of well-known triple-resonancepulse sequences which improve the dispersion of NOESY spectra. In order torecord the chemical shifts of backbone nuclei which allow a resolution ofoverlapping cross peaks, the magnetization is relayed via the scalarcoupling network either before or after the NOE mixing period. The novelpulse sequences are applied to flavodoxin from the sulfate-reducing organismDesulfovibrio vulgaris. A number of previously unassigned NOE interactionsinvolving α-, β- and amide protons can be unequivocallyidentified, suggesting that the accuracy of protein structure determinationcan be improved. Kluwer Academic Publishers, 1997 Triple-resonance NOESY nationallicence Resonance assignments nationallicence Degenerate chemical shifts nationallicence Desulfovibrio vulgaris flavodoxin nationallicence Löhr Frank Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Biozentrum N230, Marie-Curie-Strasse 9, D-60439, Frankfurt, Germany aut Rüterjans Heinz Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Biozentrum N230, Marie-Curie-Strasse 9, D-60439, Frankfurt, Germany aut Journal of Biomolecular NMR Kluwer Academic Publishers 9/4(1997-06-01), 371-388 0925-2738 9:4<371 1997 9 10858 https://doi.org/10.1023/A:1018342425634 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018342425634 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Löhr Frank Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Biozentrum N230, Marie-Curie-Strasse 9, D-60439, Frankfurt, Germany aut NATIONALLICENCE 700 1- Rüterjans Heinz Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Biozentrum N230, Marie-Curie-Strasse 9, D-60439, Frankfurt, Germany aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 9/4(1997-06-01), 371-388 0925-2738 9:4<371 1997 9 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer