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Article
Weak alignment of paramagnetic proteins warrants correction for residual CSA effects in measurements of pseudocontact shifts
Faculty of Science, Medicine and Health - Papers
  • Michael John, Australian National University
  • Ah-Young Park, Australian National University
  • Guido Pintacuda, Ecole Normale Supe Rieure de Lyon
  • Nicholas E Dixon, University of Wollongong
  • Gottfried Otting, Australian National University
RIS ID
16929
Publication Date
1-1-2005
Publication Details

John, M., Park, A., Pintacuda, G., Dixon, N. E. & Otting, G. (2005). Weak alignment of paramagnetic proteins warrants correction for residual CSA effects in measurements of pseudocontact shifts. Journal of the American Chemical Society, 127 (49), 17190-17191.

Abstract
Paramagnetic metal ions can induce molecular alignment with respect to the magnetic field. This alignment generates residual anisotropic chemical shifts (RACS) due to nonisotropic averaging over the molecular orientations. Using a 30 kDa protein−protein complex, the RACS effects are shown to be significant for heteronuclear spins with large chemical shift anisotropies, lanthanide ions with large anisotropic magnetic susceptibility tensors, and measurements at high magnetic field. Therefore, RACS must be taken into account when pseudocontact shifts are measured by comparison of chemical shifts observed between complexes with paramagnetic and diamagnetic lanthanide ions. The results are of particular importance when different pseudocontact shifts measured for the 1HN, 15N, and 13C‘ spins of a peptide group are used to restrain its orientation with respect to the electronic magnetic susceptibility tensor in structure calculations.
Citation Information
Michael John, Ah-Young Park, Guido Pintacuda, Nicholas E Dixon, et al.. "Weak alignment of paramagnetic proteins warrants correction for residual CSA effects in measurements of pseudocontact shifts" (2005)
Available at: http://works.bepress.com/nick_dixon/25/