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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F09%3A00029388%21RIV10-MSM-14310___
rdf:type
skos:Concept n18:Vysledek
dcterms:description
Using fluorescence anisotropy, we were able to compare the affinity of AtTRB proteins to fluorescently labeled DNA fragments harboring specific and nonspecific sequences and also to determine the optimal binding site by varying the size of the DNA fragments. Moreover, because fluorescence anisotropy enables the measurements to be performed in variety of experimental conditions, we managed to measure how the affinity depends on ionic strength. This allowed us to determine the electrostatic and nonelectrostatic contributions to the overall binding affinity of proteins to telomeric DNA. Based on these findings, a putative functional model of the complex between AtTRB proteins and telomeric DNA was constructed. Using fluorescence anisotropy, we were able to compare the affinity of AtTRB proteins to fluorescently labeled DNA fragments harboring specific and nonspecific sequences and also to determine the optimal binding site by varying the size of the DNA fragments. Moreover, because fluorescence anisotropy enables the measurements to be performed in variety of experimental conditions, we managed to measure how the affinity depends on ionic strength. This allowed us to determine the electrostatic and nonelectrostatic contributions to the overall binding affinity of proteins to telomeric DNA. Based on these findings, a putative functional model of the complex between AtTRB proteins and telomeric DNA was constructed.
dcterms:title
Application of fluorescence anisotropy to monitor protein binding to telomeric DNA Application of fluorescence anisotropy to monitor protein binding to telomeric DNA
skos:prefLabel
Application of fluorescence anisotropy to monitor protein binding to telomeric DNA Application of fluorescence anisotropy to monitor protein binding to telomeric DNA
skos:notation
RIV/00216224:14310/09:00029388!RIV10-MSM-14310___
n3:aktivita
n12:Z n12:P
n3:aktivity
P(GD204/08/H054), P(GP521/08/P452), Z(MSM0021622415)
n3:dodaniDat
n14:2010
n3:domaciTvurceVysledku
n6:9928758 n6:7913974 n6:9914048 n6:9227636 n6:2300303 n6:8202575
n3:druhVysledku
n4:O
n3:duvernostUdaju
n10:S
n3:entitaPredkladatele
n13:predkladatel
n3:idSjednocenehoVysledku
303777
n3:idVysledku
RIV/00216224:14310/09:00029388
n3:jazykVysledku
n17:eng
n3:klicovaSlova
Protein-DNA interaction; Arabidopsis thaliana; SMH protein; fluorescence anisotropy; electrophoretic mobility shift assay
n3:klicoveSlovo
n11:electrophoretic%20mobility%20shift%20assay n11:SMH%20protein n11:fluorescence%20anisotropy n11:Arabidopsis%20thaliana n11:Protein-DNA%20interaction
n3:kontrolniKodProRIV
[0B7F3958ABEB]
n3:obor
n7:EB
n3:pocetDomacichTvurcuVysledku
6
n3:pocetTvurcuVysledku
6
n3:projekt
n9:GD204%2F08%2FH054 n9:GP521%2F08%2FP452
n3:rokUplatneniVysledku
n14:2009
n3:tvurceVysledku
Fajkus, Jiří Procházková Schrumpfová, Petra Šultesová, Pavla Mozgová, Iva Zimmermann, Michal Hofr, Ctirad
n3:zamer
n5:MSM0021622415
n16:organizacniJednotka
14310