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Research has been conducted on the abundant bacterial DNA binding protein Fis. The parameters affecting Fis subunit exchange in solution and the role of the dimer interface flexibility in the formation and stability of the Fis-DNA complex have been investigated and discussed.

Research has been conducted on the non-histone chromatin-associated Saccharomyces cerevisiae protein Nhp6A. Results indicate that this protein binds to duplex DNA's cisplatin intrastrand cross-links.

The first identification of novel Fis binding sites was made through DNA splitting mediated by the chimeric nuclease Fis-1,10-phenanthroline-copper(I). The chemical nuclease (OP)2CU+ is fastened to residue 73 of the protein with the use of the acetyl-beta-alanylamino linker N73C-AOP. Thus, two high-affinity Fis binding sites in the lacP and oriE sites of the pUC19 vector are identified. The DNA scission efficiency is dependent on the high-affinity binding of the chelate to the minor groove.

Micromechanical analysis of the binding of DNA-bending proteins HMGB1, NHP6A, and HU is investigated using DNA micromanipulation. The results show that the stability of the DNA-protein complexes is dependent on the protein concentration during the binding.

Complementary information was provided by the use of isotopically labeled DNA in a protein-DNA complex. The results not only provided confirmation of the intermolecular NOEs obtained from spectra of complexes with isotopically labeled protein, but also allowed unambiguous assignment of intermolecular crosspeaks which could not have been otherwise resolved. For non-sequence-specific DNA-protein interactions, this is particularly important.