Modeling Cu(II) Binding to Peptides Using the Extensible Systematic Force Field
Figure 3
(a) The structure of CuP34 for Cu024 symmetry following energy minimization. The peptide backbone is shown in yellow, random coil regions in green, and β-turn regions in blue. Histidine residues are in red. The Cu(II) ion is in magenta. (b) Superposition of CuP34 structures obtained for Cu024 and Cu025 symmetries showing that they have very similar conformations.
