caa a22 4500 477136125 CHVBK 20180405111718.0 cr unu---uuuuu 170330e19970901xx s 000 0 eng 10.1023/A:1018355327792 doi (NATIONALLICENCE)springer-10.1023/A:1018355327792 Application of H(N)CA,CO-E.COSY experiments for calibrating the φ angular dependences of vicinal couplings J(C′i−1,Hiα), J(C′i−1,Ciβ) and J(C′i−1,C′i) in proteins [Elektronische Daten] [Frank Löhr, Markus Blümel, Jürgen Schmidt, Heinz Rüterjans] A triple-resonance NMR technique suitable for the determination ofcarbonyl-related couplings in polypeptide systems is introduced. Theapplication of three novel pulse sequences to uniformly13C/15N-enriched proteins yields E.COSY-likemultiplet patterns exhibiting either one of the3J(C′i−1,Hi α), 3J(C′i−1,Ci β) and3J(C′i−1,C′i)coupling constants in the indirectly detected 13C′dimension, depending on the passive spin selected. The experiments aredemonstrated with oxidized flavodoxin from Desulfovibrio vulgaris. On thebasis of the J-values measured and the backbone φ-angles derived from ahigh-resolution X-ray structure of the protein, the three associated Karplusequations were reparametrized. The root-mean-square differences between theexperimental coupling constants and those predicted by the optimized Karpluscurves are 0.41, 0.33 and 0.32 Hz for3J(C′i−1,Hi α),3J(C′i−1,Ci β) and3J(C′i−1,C′i),respectively. The results are compared with the Karplus parameters previouslypublished for the same couplings. Kluwer Academic Publishers, 1997 Vicinal coupling constants nationallicence φ Torsion angle nationallicence Karplus parametrization nationallicence Desulfovibrio vulgaris flavodoxin nationallicence Isotopic labelling nationallicence Löhr Frank Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Marie-Curie-Strasse 9, Biozentrum N230, D-60439, Frankfurt, Germany aut Blümel Markus Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Marie-Curie-Strasse 9, Biozentrum N230, D-60439, Frankfurt, Germany aut Schmidt Jürgen Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Marie-Curie-Strasse 9, Biozentrum N230, D-60439, Frankfurt, Germany aut Rüterjans Heinz Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Marie-Curie-Strasse 9, Biozentrum N230, D-60439, Frankfurt, Germany aut Journal of Biomolecular NMR Kluwer Academic Publishers 10/2(1997-09-01), 107-118 0925-2738 10:2<107 1997 10 10858 https://doi.org/10.1023/A:1018355327792 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018355327792 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Löhr Frank Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Marie-Curie-Strasse 9, Biozentrum N230, D-60439, Frankfurt, Germany aut NATIONALLICENCE 700 1- Blümel Markus Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Marie-Curie-Strasse 9, Biozentrum N230, D-60439, Frankfurt, Germany aut NATIONALLICENCE 700 1- Schmidt Jürgen Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Marie-Curie-Strasse 9, Biozentrum N230, D-60439, Frankfurt, Germany aut NATIONALLICENCE 700 1- Rüterjans Heinz Institut für Biophysikalische Chemie, Johann Wolfgang Goethe Universität Frankfurt am Main, Marie-Curie-Strasse 9, Biozentrum N230, D-60439, Frankfurt, Germany aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 10/2(1997-09-01), 107-118 0925-2738 10:2<107 1997 10 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer