Structure refinement of cyclosporin A in chloroform by using RDCs measured in a stretched PDMS-gel

Jochen Klages, Cajetan Neubauer, Murray Coles, Horst Kessler, Burkhard Luy

Research output: Contribution to journalArticlepeer-review

74 Scopus citations

Abstract

New developments concerning alignment media for apolar solvents like chloroform make it possible to measure anisotropic parameters such as residual dipolar couplings (RDCs) at relatively low concentrations and natural isotopic abundance. As RDCs provide structural restraints with respect to an external coordinate system, long-range structural arrangements of the time-averaged structure can be determined with high precision. The method is demonstrated on the well-studied cyclo-undecapeptide Cyclosporin A (CsA), for which crystal and conventionally derived NMR structures are available. Neither crystal nor NMR structure are consistent with heteronuclear DCH RDCs measured in a stretched poly(dimethylsiloxane) gel, and refinement by using the anisotropic parameter results in a highly defined structure with a slightly changed backbone conformation. The applied methods and interpretation of the structural model are discussed.

Original languageEnglish
Pages (from-to)1672-1678
Number of pages7
JournalChemBioChem
Volume6
Issue number9
DOIs
StatePublished - Sep 2005

Keywords

  • Cyclosporin A
  • NMR spectroscopy
  • Partial alignment
  • Residual dipolar couplings
  • Structure elucidation

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