Number of the records: 1
Applications of phasor plots to in vitro protein studies
- 1.
SYSNO ASEP 0367712 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Applications of phasor plots to in vitro protein studies Author(s) James, N. G. (US)
Ross, J. A. (US)
Štefl, Martin (UFCH-W)
Jameson, D. M. (US)Source Title Analytical Biochemistry. - : Elsevier - ISSN 0003-2697
Roč. 410, č. 1 (2011), s. 70-76Number of pages 7 s. Language eng - English Country US - United States Keywords protein fluorescence ; kinetics ; lifetimes Subject RIV CF - Physical ; Theoretical Chemistry R&D Projects LC06063 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z40400503 - UFCH-W (2005-2011) UT WOS 000286711300011 DOI 10.1016/j.ab.2010.11.011 Annotation 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. Workplace J. Heyrovsky Institute of Physical Chemistry Contact Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Year of Publishing 2012
Number of the records: 1