[Reaction between synthetic fragment of histone F2al and the protamines iridine and salmine with DNA].
The interaction of basic oligopeptides--F2aI histone, iridine and salmine protamines synthetic fragments with DNA has been studied by the methods of thermal denaturation, circular dichroism and equilibrium dialysis. All the peptides investigated are albe to stabilize the DNA helix and change its conformation. This ability grows with the increase of a number of basic residues in the peptide molecule and decreases when there is a serin residue on the end. The binding of the peptide with DNA obtains a cooperative character if 4--6 arginine clusters are present in the molecule. The comparison of the binding coefficient with the thermal denaturation data allowed to propose an important role of nonelectrostatic forces on the binding of the peptides to DNA.
D000595:Amino Acid Sequence; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D002942:Circular Dichroism; D004247:DNA; D006657:Histones; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D009842:Oligopeptides; D011479:Protamines; D012473:Salmine; D013696:Temperature
D006657:Histones; D009842:Oligopeptides; D011479:Protamines; D004247:DNA; D012473:Salmine
Izuchenie vzaimodeĭstviia sinteticheskikh fragmentov gistona F2al protaminov iridina i salmina s DNK.