Linker histones (H1) are a family of lysine-rich proteins that bind to or near the point at which DNA enters and exits the nucleosomal core. A number of studies have shown that H1 expression levels are altered in cancer and that variant-specific changes can be observed in different tumor cells. Although several crystal structures are published for core-histone/DNA complex (nucleosome), the location of linker histone and its interactions are poorly understood. This study attempts to answer several questions regarding the interactions of histone H1 with double stranded partner DNA. Preliminary NMR assignments of this protein have been determined. We also investigated the structural changes in histone H1.0 globular domain induced by DNA binding. During the course of this project it was observed that subtle changes in pH could affect NMR spectral quality. We investigated the pH dependence of the protein stability by performing Circular Dichroism (CD) experiments.