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  • 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. (en)
Title
  • Application of fluorescence anisotropy to monitor protein binding to telomeric DNA
  • Application of fluorescence anisotropy to monitor protein binding to telomeric DNA (en)
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  • Application of fluorescence anisotropy to monitor protein binding to telomeric DNA
  • Application of fluorescence anisotropy to monitor protein binding to telomeric DNA (en)
skos:notation
  • RIV/00216224:14310/09:00029388!RIV10-MSM-14310___
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  • P(GD204/08/H054), P(GP521/08/P452), Z(MSM0021622415)
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  • 303777
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  • RIV/00216224:14310/09:00029388
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  • Protein-DNA interaction; Arabidopsis thaliana; SMH protein; fluorescence anisotropy; electrophoretic mobility shift assay (en)
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  • [0B7F3958ABEB]
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  • Fajkus, Jiří
  • Mozgová, Iva
  • Hofr, Ctirad
  • Zimmermann, Michal
  • Procházková Schrumpfová, Petra
  • Šultesová, Pavla
http://linked.open...n/vavai/riv/zamer
http://localhost/t...ganizacniJednotka
  • 14310
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