Histones play an important role in gene regulation and expression. DNA is wound around these proteins and chemical modifications to the side chains of histone amino acids can result in changes in the interaction between the histones and DNA. This may cause alterations in gene expression as the DNA can become either more or less attracted to the histone which in turn alters the accessibility of the gene loci around where the modification occurs. The project undertaken in this thesis involves the synthesis of the N-terminal tail of two major histones, H3 and H4, through solid phase peptide synthesis. The N-terminal tail was chosen as it undergoes extensive modifications as it is less constrained by the secondary and tertiary structure of the protein. These peptides can later be used in biochemical assays in the presence of enzymes that catalyze histone modifications as well as in assays to screen drug inhibitors of these enzymes. This will allow for the manipulation of the post-translational modification process of histones and, potentially, the regulation of gene expression in diseases.