Folding of the SPKK rich peptide in the presence of the octa-oligonucleotide

Abstract

The nucleosome contains of 200 base pairs of DNA complexed with four core histone complex: H2A, H2B, H3, and H4. The fifth histone species, the H1 histone, interacts with linker DNA connecting neighbouring nucleosomes. We have studied the influence of the phosphorylation on the interactions of a repeating unit 15 residues long, containing the SPKK motif, the motif thought to induce turn along peptides sequences, enclosed within the trout testis H1 C-terminal domain with octanucleotide by means of the thermal denaturation and CD technique. The results indicate that the peptide preferentially binds to a single stranded oligonucleotide. It has been shown further that there is no β structure present but a distorted helical structure has been detected.