MM-EPR method

The validity of the MM-EPR method is further demonstrated with the two structurally related dicopper(II) complexes A and B whose calculated structures (MM-EPR) are presented in Fig. 9.6. For both bis-macrocyclic ligands two identical... 

Cyclic peptides can be viewed as a step on the way from the modeling of unconstrained peptides to folded proteins. The copper(II) complexes of cyclic octapeptides have been investigated by molecular mechanics and EPR spectroscopy (M M -E P R), and the structures were found to be in accord with those of closely related complexes (see also Chapter 10) [262,483]. More recently, the MM-EPR method has been extended by DFT [410], and used to characterize the mono- and dicopper(II) complexes of the smaller cyclic peptide Westiallamide and some analogues [484]. Similar combined approaches are also applicable to metalloproteins. 

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