E-mail a Wiley Online Library Link

Jochen Klages, Cajetan Neubauer, Murray Coles, Horst Kessler and Burkhard Luy Structure Refinement of Cyclosporin A in Chloroform by Using RDCs Measured in a Stretched PDMS-Gel ChemBioChem 6

Version of Record online: 1 SEP 2005 | DOI: 10.1002/cbic.200500146

Thumbnail image of graphical abstract

Structural refinement of a cyclic peptide in chloroform was achieved by using residual dipolar couplings (RDCs) as angular restraints. These couplings provide long-range structural information and are measurable at relatively low concentrations and natural isotope abundance. The method is demonstrated on the well-studied cyclo-undecapeptide Cyclosporin A. Here the RDC-refined structure is shown in blue.

Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf

Required = Required Field