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Techniques involving NMR-molecular dynamics and relaxation matrix refinement were utilised in the structure analysis of complexes produced from Mg2+-coordinated mithramycin dimer binding to self-complementary d(T-G-G-C-C-A) and d(T-C-G-C-G-A) duplexes. The molecular structure of the mithramycin dimer d(T-C-G-C-G-A) reveals a two-fold center of symmetry. The aglycon C-8 hydroxyl oxygens are hydrogen bonded to guanine amino protons in the complex due to the positioning of divalent cation coordinated glycons, opposite the central (G3-C4). (G3-C4) segment.

The design of a new peptide motif that is a hybrid of Beta-hairpin and Beta-helical supersecondary structures is described. The results of characterization of the peptide motif confirm success of the design of the motif and emphasize that hybrid [Beta]-hairpin/[Beta]-helical constructs described were characterized only in nonpolar organic solvents.

A functional model for the oxidation of manganese (Mn2+) in manganese peroxidase (MnP) through the enlistment of inherent oxidizing potential of another peroxidase was examined. The construction and structural properties of Mn2+ binding sites near the heme of cytochrome c peroxidase (CCP) were described. The CCP demonstrated 20% amino acid sequence identity and structural similarity to MnP even without the binding sites observed in MnP. The findings confirmed that the presence of Mn2+ caused paramagnetic broadening of two proton resonances in the upfield area of the spectrum.