Solution structure of a designed cyclic peptide ligand for nickel and copper ions |
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Authors: | Matthew R Eshelman Amanda R AldousKosh P Neupane Joshua A Kritzer |
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Institution: | Department of Chemistry, Tufts University, 62 Talbot Avenue, Medford, MA 02155, United States |
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Abstract: | Nuclear magnetic resonance (NMR) spectroscopy was used to study a cyclic peptide derived from the amino-terminal copper-and-nickel-binding (ATCUN) motif. The three-dimensional structure of the unliganded peptide in aqueous solution was solved by simulated annealing using distance constraints derived from Nuclear Overhauser Effects. A structural model for the Ni(II)-bound complex was also produced based on NMR evidence and prior spectroscopic data, which are consistent with crystal structures of linear ATCUN complexes. Structural interpolation, or ‘morphing’, was used to understand the transition of this highly structured cyclic peptide from its unliganded structure to its metal-ion-bound structure. |
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Keywords: | ATCUN Cyclic peptide NMR Modeling Ni(II) binding |
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