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

Kritzer, Joshua A.
Eshelman, Matthew R.
Aldous, Amanda.
Neupane, Kosh P.
2014.

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

Subjects
Peptides.
Modeling.
Nuclear magnetic resonance.
Tufts University. Department of Chemistry.
Permanent URL
http://hdl.handle.net/10427/013735
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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