TY - JOUR
T1 - Quantitative footprinting analysis of the netropsin-dna interaction
AU - Ward, Brian
AU - Rehfuss, Robert
AU - Dabrowiak, Janies C.
N1 - Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.
PY - 1987/4
Y1 - 1987/4
N2 - The results of a series of quantitative footprinting experiments of the netropsin-DNA interaction as studied using two different DNA cleaving probes, the enzyme DNase I and a cationic manganese porphyrin complex, are described. Plots of the relative change in oligonucleotide concentration as a function of drug concentration, covering -110 base pairs of a DNA restriction fragment, revealed netropsin induced changes in the cleavage rates of both probes. These appeared as inhibitions for the binding sites, enhancements where no binding took place, and enhancement/inhibitions for the weak binding sites. Determination of the concentration of drug necessary to reduce the amount of a particular oligomer to half of its initial value allowed a ranking of the affinities of the various binding sites on the fragment. In addition to uncovering the location of a number of overlapping netropsin binding sites, the data allowed additional insight on the manner in which both probes alter their DNA cleavage rates in the drug-footprinting experiment.
AB - The results of a series of quantitative footprinting experiments of the netropsin-DNA interaction as studied using two different DNA cleaving probes, the enzyme DNase I and a cationic manganese porphyrin complex, are described. Plots of the relative change in oligonucleotide concentration as a function of drug concentration, covering -110 base pairs of a DNA restriction fragment, revealed netropsin induced changes in the cleavage rates of both probes. These appeared as inhibitions for the binding sites, enhancements where no binding took place, and enhancement/inhibitions for the weak binding sites. Determination of the concentration of drug necessary to reduce the amount of a particular oligomer to half of its initial value allowed a ranking of the affinities of the various binding sites on the fragment. In addition to uncovering the location of a number of overlapping netropsin binding sites, the data allowed additional insight on the manner in which both probes alter their DNA cleavage rates in the drug-footprinting experiment.
UR - http://www.scopus.com/inward/record.url?scp=0023226908&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023226908&partnerID=8YFLogxK
U2 - 10.1080/07391102.1987.10507672
DO - 10.1080/07391102.1987.10507672
M3 - Article
C2 - 2855921
AN - SCOPUS:0023226908
SN - 0739-1102
VL - 4
SP - 685
EP - 695
JO - Journal of Biomolecular Structure and Dynamics
JF - Journal of Biomolecular Structure and Dynamics
IS - 5
ER -