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Structure-independent cross-validation between residual dipolar couplings originating from internal and external orienting media

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Abstract

Lanthanide-substituted calcium binding proteins are known to partially orient in high magnetic fields. Orientation provides residual dipolar couplings (rdc's). Two of these systems, Tm3+- and Dy3+-substituted calbindin D9k, dissolved in an external orienting medium (nonionic liquid crystalline phase) provide rdc values which are the sum of those induced by the lanthanides and by the liquid crystalline phase on the native calcium binding protein. This structure-independent check shows the innocence of the orienting medium with respect to the structure of the protein in solution. Furthermore, the simultaneous use of lanthanide substitution and external orienting media provides a further effective tool to control and tune the orientation tensor.

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Authors and Affiliations

  1. Magnetic Resonance Center CERM, Department of Chemistry, University of Florence, Via Luigi Sacconi, 6, 50019, Sesto Fiorentino, Italy

    Renato Barbieri, Ivano Bertini, Yong-Min Lee, Claudio Luchinat & Aldrik H. Velders

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  1. Renato Barbieri
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  2. Ivano Bertini
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  3. Yong-Min Lee
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  4. Claudio Luchinat
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  5. Aldrik H. Velders
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Barbieri, R., Bertini, I., Lee, YM. et al. Structure-independent cross-validation between residual dipolar couplings originating from internal and external orienting media. J Biomol NMR 22, 365–368 (2002). https://doi.org/10.1023/A:1014980101965

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