AIM To further characterize the structure and nucleic acid binding properties of the 195 amino acid small delta antigen,S-HDAg,a study was made of a truncated form of S-HDAg,comprising amino acids 61-195(Δ60HDAg),thus lacking the domain considered necessary for dimerization and higher order multimerization.METHODS Circular dichroism,and nuclear magnetic resonance experiments were used to assess the structure ofΔ60HDAg.Nucleic acid binding properties were investigated by gel retardation assays.RESULTS Results showed that the truncatedΔ60HDAg protein is intrinsically disordered but compact,whereas the RNA a dynamic helical conformation.We also found thatΔ60HDAg fails to multimerize but still contains nucleic acid binding activity,indicating that multimerization is not essential for nucleic acid binding.Moreover,in agreement with what has been previously reported for full-length protein,no apparent specificity was found for the truncated protein regarding nucleic acid binding.CONCLUSION Taken together these results allowed concluding thatΔ60HDAg is intrinsically disordered but compact;Δ60HDAg is not a multimer but is still capable of nucleic acid binding albeit without apparent specificity.