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Research demonstrates the association of complementing polar groups with buried and surface positions of proteins in protein folding as exemplified by a two-stranded coiled-coil design of the ACID-p1/BASE-p1 heterodimer. Data indicate that position-a Lys residues and Lys-Glu polar interactions impart a high level of structural feature to the heterodimer.

A nondegenerative recognition code table based on amino acid-DNA base interactions in DNA complexes with DNA-binding proteins is presented. The code table can be used to identify the specific amino acid, at a specific position of the alpha-helical region of zinc-finger domain, from the overlapping target sequence in a given DNA target.

Research suggests that the open and closed conformations of maltose-binding protein facilitate variable copper-copper distance formation. A mutation in the hinge region of the protein leads to the formation of a binuclear copper center, which simulates oxy-hemocyanin upon reacting with hydrogen peroxide.