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  • Coupling constants  (1)
  • Karplus parametrization  (1)
  • 1995-1999  (2)
  • 1985-1989
  • 1965-1969
  • 1
    Electronic Resource
    Electronic Resource
    Determination of heteronuclear three-bond J-coupling constants in peptides by a simple heteronuclear relayed E.COSY experiment (1995)
    Springer
    Journal of biomolecular NMR 6 (1995), S. 95-105 
    Details
    ISSN: 1573-5001
    Keywords: 2D heteronuclear NMR ; Isotope labeling ; Coupling constants ; Antamanide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A simple heteronuclear relayed E.COSY pulse sequence with a minimum number of pulses is proposed for the quantitative determination of heteronuclear three-bond J-coupling constants in uniformly 13C-enriched polypeptide samples. Numerous heteronuclear three-bond coupling constants, including $${}^3{\text{J}}_{{\text{H}}^{\text{N}} {\text{C}}'} $$ , $${}^3{\text{J}}_{{\text{H}}^{\text{N}} {\text{C}}^\beta } $$ , $${}^3{\text{J}}_{{\text{H}}^\beta {\text{C}}'} $$ , and $${}^3{\text{J}}_{{\text{H}}^\alpha {\text{C}}^\gamma } $$ , can be determined for each residue from a single heteronuclear relayed E.COSY spectrum. Couplings relevant for stereospecific assignments as well as for the determination of dihedral angles in the amino acid backbone and in side chains are obtained. The method is demonstrated on the uniformly 13C-enriched decapeptide antamanide (-Val1-Pro2-Pro3-Ala4-Phe5-Phe6-Pro7-Pro8-Phe9-Phe10-).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00417495
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  • 2
    Electronic Resource
    Electronic Resource
    Application of H(N)CA,CO-E.COSY experiments for calibrating the φ angular dependences of vicinal couplings J(C′i−1,Hi α), J(C′i−1,Ci β) and J(C′i−1,C′i) in proteins (1997)
    Springer
    Journal of biomolecular NMR 10 (1997), S. 107-118 
    Details
    ISSN: 1573-5001
    Keywords: Vicinal coupling constants ; φ Torsion angle ; Karplus parametrization ; Desulfovibrio vulgaris flavodoxin ; Isotopic labelling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018355327792
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