title: 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 beta structure present but a distorted helical structure has been detected.
authors.affiliation: European Molecular Biology Laboratory, Heidelberg, Germany.
authors.forename: I Z
authors.initials: IZ
authors.lastname: Zubrzycki
authors.forename: L
authors.initials: L
authors.lastname: Bohm
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D004247:DNA / Q000737:chemistry*; D006657:Histones / Q000737:chemistry*; D008297:Male; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D010766:Phosphorylation; D011487:Protein Conformation; D017510:Protein Folding; D012474:Salmon; D013094:Spermatozoa
chemical_list: D006657:Histones; D009838:Oligodeoxyribonucleotides; D010446:Peptide Fragments; D004247:DNA