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  • In a recent article, we described the application of phasor analysis to fluorescence intensity decay data on in vitro samples. As detailed in that article, this method provides researchers with a simple graphical method for viewing lifetime data that can be used to quantify individual components of a mixture as well as to identify excited state reactions. In the current article, we extend the use of in vitro phasor analysis to intrinsic protein fluorescence. We show how alterations in the excited state properties of tryptophan residues are easily visualized using the phasor method. Specifically, we demonstrate that protein-ligand and protein-protein interactions can result in unique shifts in the location of phasor points, indicative of protein conformational changes. Application of the method to a rapid kinetic experiment is also shown.
  • In a recent article, we described the application of phasor analysis to fluorescence intensity decay data on in vitro samples. As detailed in that article, this method provides researchers with a simple graphical method for viewing lifetime data that can be used to quantify individual components of a mixture as well as to identify excited state reactions. In the current article, we extend the use of in vitro phasor analysis to intrinsic protein fluorescence. We show how alterations in the excited state properties of tryptophan residues are easily visualized using the phasor method. Specifically, we demonstrate that protein-ligand and protein-protein interactions can result in unique shifts in the location of phasor points, indicative of protein conformational changes. Application of the method to a rapid kinetic experiment is also shown. (en)
Title
  • Applications of phasor plots to in vitro protein studies
  • Applications of phasor plots to in vitro protein studies (en)
skos:prefLabel
  • Applications of phasor plots to in vitro protein studies
  • Applications of phasor plots to in vitro protein studies (en)
skos:notation
  • RIV/61388955:_____/11:00367712!RIV12-AV0-61388955
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LC06063), Z(AV0Z40400503)
http://linked.open...iv/cisloPeriodika
  • 1
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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  • 186899
http://linked.open...ai/riv/idVysledku
  • RIV/61388955:_____/11:00367712
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • protein fluorescence; kinetics; lifetimes (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [3BD003574901]
http://linked.open...i/riv/nazevZdroje
  • Analytical Biochemistry
http://linked.open...in/vavai/riv/obor
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  • 410
http://linked.open...iv/tvurceVysledku
  • James, N. G.
  • Jameson, D. M.
  • Ross, J. A.
  • Štefl, Martin
http://linked.open...ain/vavai/riv/wos
  • 000286711300011
http://linked.open...n/vavai/riv/zamer
issn
  • 0003-2697
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/j.ab.2010.11.011
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