A photo-CIDNP study of the interaction of oligonucleotides with gene-5 protein of bacteriophage M13.
It is shown that photo-CIDNP effects (CIDNP, chemically induced dynamic nuclear polarization) can be generated in the 360-MHz proton NMR spectrum of gene-5 protein from bacteriophage M13. This technique is used to determine the number of tyrosyl residues at the surface of the protein and to assign the resonances from the 3,5-ring protons of these residues. The DNA-binding site of the protein is investigated by formation of complexes with oligonucleotides. Complex formation leads to shifting and/or quenching of the photo-CIDNP emission signals of the surface tyrosines, implying that they are involved in DNA-protein interaction. These experiments are complemented by studying the complex formation of Lys-Tyr-Lys to poly(A).
D001665:Binding Sites; D003090:Coliphages; D004926:Escherichia coli; D005814:Genes, Viral; D009682:Magnetic Resonance Spectroscopy; D009841:Oligonucleotides; D009843:Oligoribonucleotides; D011485:Protein Binding; D014764:Viral Proteins
D009841:Oligonucleotides; D009843:Oligoribonucleotides; D014764:Viral Proteins