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Article
Measurement of dissociation constants of high-molecular weight protein-protein complexes by transferred 15N-relaxation
Faculty of Science, Medicine and Health - Papers
  • Xun Cheng Su, Australian National University
  • Slobodan Jergic, University of Wollongong
  • Kiyoshi Ozawa, University of Wollongong
  • Nicolas Dale Burns, Australian National University
  • Nicholas E Dixon, University of Wollongong
  • Gottfried Otting, Australian National University
RIS ID
16853
Publication Date
1-1-2007
Publication Details

Su, X. Cheng., Jergic, S., Ozawa, K., Burns, N. D., Dixon, N. E. & Otting, G. (2007). Measurement of dissociation constants of high-molecular weight protein-protein complexes by transferred 15N-relaxation. Journal of Biomolecular N M R, 38 (1), 65-72.

Abstract
The use of 15N-relaxation data for determination of the dissociation constant of a protein–protein complex is proposed for the situation where a 15N-labeled protein is bound to an unlabeled protein of high molecular weight, and the chemical exchange between bound and free protein is fast on the NMR time scale. The approach is shown to be suitable for estimating dissociation constants in the micromolar to millimolar range, using protein solutions at relatively low concentration. An example is shown for the interaction between two subunits from the Escherichia coli DNA polymerase III complex, involving a 15N-labeled fragment of the C-terminal domain of the τ subunit (15 kDa) and the unlabeled α subunit (130 kDa).
Citation Information
Xun Cheng Su, Slobodan Jergic, Kiyoshi Ozawa, Nicolas Dale Burns, et al.. "Measurement of dissociation constants of high-molecular weight protein-protein complexes by transferred 15N-relaxation" (2007)
Available at: http://works.bepress.com/nick_dixon/5/