Solution structure of a designed cyclic peptide ligand for nickel and copper ions.

Kritzer, Joshua A.
Eshelman, Matthew R.
Aldous, Amanda.
Neupane, Kosh P.

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 ... read more

Nuclear magnetic resonance.
Tufts University. Department of Chemistry.
Permanent URL
Original publication
Eshelman, M.R., Aldous, A.R., Neupane, K.P., and Kritzer, J.A. Solution Structure of a Designed Cyclic Peptide Ligand for Nickel and Copper Ions. Tetrahedron 2014 70(42), 7651-7654. doi:10.1016/j.tet.2014.07.083.
ID: tufts:23302
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