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Protein Structure Refinement using Residual Dipolar Couplings

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Protein NMR for the Millennium

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 20))

Abstract

Residual dipolar couplings arise from small degrees of alignment of molecules in a magnetic field. Media employed for imparting alignment onto biomolecules lacking sufficient magnetic susceptibility anisotropies themselves comprise dilute aqueous phospholipid bicelles, colloidal suspensions of rod-shaped viruses and lamellar phases of quasiternary surfactant systems. The magnitude of the residual dipolar couplings depends upon the degree of ordering and allows the determination of the corresponding internuclear vectors with respect to the molecule’s alignment frame. Inclusion of dipolar constraints into NMR structure calculations leads to improved accuracy of the resulting structures, especially in cases where the information content provided by traditional NOE constraints is limited. This chapter describes the different media used for alignment and the application of dipolar coupling information for protein structure refinement and fold determination.

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Gronenborn, A.M. (2002). Protein Structure Refinement using Residual Dipolar Couplings. In: Krishna, N.R., Berliner, L.J. (eds) Protein NMR for the Millennium. Biological Magnetic Resonance, vol 20. Springer, Boston, MA. https://doi.org/10.1007/0-306-47936-2_8

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  • DOI: https://doi.org/10.1007/0-306-47936-2_8

  • Publisher Name: Springer, Boston, MA

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