PMID: 39645Jul 1, 1979

The binding of Arg- and Lys-peptides to single stranded polyribonucleotides and its effect on the polymer conformation

Biophysical Chemistry
D Porschke


The interactions between basic oligopeptides (Lys2, Lys3, Arg2 and Arg3) and single stranded polynucleotides (poly(A), poly(C), poly(I) and poly(U) were investigated at low ion concentration by UV spectroscopy, circular dichroism and field jump relaxation. Various domains of binding were detected: 1) High concentrations (up to 1 mM) of some peptides induce opalescence followed by coacervation. Arg3 causes coacervation in all polynucleotides used, yet Lys3 only in poly(I). In the case of poly(I) the threshold concentration for coacervation is much lower for Arg3 (150 muM) than for Lys3 (500 muM). 2) Medium concentrations (greater than 10 muM) of Arg3 and Lys3 induce helix formation in poly(U). In the case of poly(I) cooperative helix formation is only induced by Lys3, but not by Arg3. 3) The onset of peptide association is observed at very low peptide concentrations (greater than or equal to 1muM) already by using the field jump method. The association is reflected by a relaxation process, that can be described by a single exponential within experimental accuracy. Measurements of relaxation time constants as a function of the peptide concentration provide information on the association constants K, the number of nucleotide resid...Continue Reading


Feb 1, 1993·Protein Science : a Publication of the Protein Society·F Dib-HajjD P Giedroc
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Related Concepts

Molecular Helix
Adenine Polynucleotides
Complex (molecular entity)
Helix (Snails)
Recombination, Genetic

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