[Comparative study of synthetic peptide fragments of histones H2B].

Oligopeptides of the N-terminal end of H2B histone with different molecular weights and amino acid sequences are studied by the CD method and X-ray analysis. Characteristic peculiarities of CD-spectra and position of diffraction maximums in X-ray diagrams in all the studied oligopeptides show that their conformation by the structure is similar to the extended left--handed helix of polyproline II. The investigation of CD-spectra under different conditions showed the dependence of the stability of "proII" conformation on the oligopeptide chain length. Their spectral and conformational properties may be due to peculiarities of their amino acid composition.