The shape of thermal denaturation profiles for F1 nucleohistone was observed to be a funtion of the ion content of the medium. The temperature derivative profile of denaturation was bimodal at 0.01 M salt but unimodal at low salt. This behavior was not a function of the method of reconstitution, the protein concentration, or the non-ionic components of the solvent. Plots of T m values vs salt concentration indicated that neither of the split peaks was directly related to the single maximum in the derivative profile at low salt. Circular dichroic spectra were not casually related to the profile splitting phenomenon studied by thermal denaturation. The unexpected ion dependence of the denaturation profile is presumed to result from electrostatic factors and the existence of at least two modes of binding of F1 histone to DNA.