Interaction of lac repressor with alternating poly d (A-T) and poly d (G-C). Circular dichroism studies.
The binding of lac repressor to poly d(A-T) and d(G-C) has been studied using circular dichroism. The results indicate that the binding induces the same conformational change of both polynucleotides and perturbs the same number of nucleic acid bases (28 bases). It is shown that in 0.1 M phosphate buffer the CD measurement can be used to determine the binding constant of lac repressor to poly d(A-T). Competition experiments performed at various salt concentrations show that the stronger interaction of lac repressor for poly d(A-T) than for poly d(G-C) is based on difference in the dissociation rate of the complexes whereas the association rate for both polymers are similar.
D001665:Binding Sites; D002942:Circular Dichroism; D004926:Escherichia coli; D007700:Kinetics; D009690:Nucleic Acid Conformation; D011067:Poly dA-dT; D011089:Polydeoxyribonucleotides; D011485:Protein Binding; D011487:Protein Conformation; D012097:Repressor Proteins; D014157:Transcription Factors
D011089:Polydeoxyribonucleotides; D012097:Repressor Proteins; D014157:Transcription Factors; D011067:Poly dA-dT; C019530:poly(dC-dG)