Measurement of one bond dipolar couplings through lanthanide-induced orientation of a calcium-binding protein [4]

Journal of the American Chemical Society

Volumn 121, Issue 38, 1999, Pages 8947-8948

  Contreras, Miquel Àngel ^a   Ubach, Josep ^b   Millet, Òscar ^a   Rizo, Josep ^b   Pons, Miquel ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; LANTHANIDE; SYNAPTOTAGMIN; YTTERBIUM;

AMINO ACID SUBSTITUTION; ANISOTROPY; BINDING AFFINITY; CHEMICAL BOND; CHEMICAL REACTION; CRYSTAL STRUCTURE; DIPOLE; LETTER; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION;

EID: 0033615311     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja990566r     Document Type: Letter

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33. Cross-correlation between dipole-dipole relaxation mechanisms and Curie spin relaxation, due to dipolar coupling of each nucleus with the time- averaged electron magnetic moment induced by the external magnetic field, has been shown to occur in paramagnetic molecules (Bertini, I.; Luchinat, C.; Tarchi, D. Chem. Phys. Lett. 1993, 203, 445-449; Maeller, L.; Mulder, F. A.; Kowalewski, J. J. Magn. Reson., Ser. A 1995, 117, 220-227). This cross-correlation could also induce dynamic frequency shifts when paramag-netic and diamagnetic systems are compared, but for the long nucleus-metal distances of the NH groups analyzed in this work, this contribution has been found to be negligible.