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Applications of phasor plots to in vitro protein studies
- 1.0367712 - ÚFCH JH 2012 RIV US eng J - Journal Article
James, N. G. - Ross, J. A. - Štefl, Martin - Jameson, D. M.
Applications of phasor plots to in vitro protein studies.
Analytical Biochemistry. Roč. 410, č. 1 (2011), s. 70-76. ISSN 0003-2697. E-ISSN 1096-0309
R&D Projects: GA MŠMT(CZ) LC06063
Institutional research plan: CEZ:AV0Z40400503
Keywords : protein fluorescence * kinetics * lifetimes
Subject RIV: CF - Physical ; Theoretical Chemistry
Impact factor: 2.996, year: 2011
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.
Permanent Link: http://hdl.handle.net/11104/0202290
Number of the records: 1