[Interactions of gene 5 protein of bacteriophage f1 with oligonucleotides of a certain composition and sequence].
Interaction of gene 5 protein of bacteriophage f1 with a set of oligodeoxyribonucleotides (including those with 1,N6-ethenoadenine), which simulate a site of attachment of protein on DNA has been studied. The tyrosine and ethenoadenine fluorescence and CD of the complexes of the protein with the oligonucleotides have been measured. It has been revealed that the stoichiometry of the complexes depends on the protein--oligonucleotide ratio. It is demonstrated that protein binding changes the degree of hydration of the oligonucleotides and the geometry of stacking, without marked unstacking. Tyrosine residues partially intercalate in the oligonucleotide. It is possible that one of the tyrosines sits between the second and the third and one of the phenylalanines--between the third and the forth bases, of the pentanucleosidetetraphosphate from the 5'-end.
D001483:Base Sequence; D002942:Circular Dichroism; D003090:Coliphages / Q000378:metabolism*; D007700:Kinetics; D009690:Nucleic Acid Conformation; D009838:Oligodeoxyribonucleotides; D009841:Oligonucleotides; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000378:metabolism*
D009838:Oligodeoxyribonucleotides; D009841:Oligonucleotides; D014764:Viral Proteins
Bzaimodeĭstvie belka gena 5 bakteriofaga f1 s oligonukleotidami zadannoga sostava i posledovatel'nosti.