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Proceedings Article

A photophysical study of two fluorogen-activating proteins bound to their cognate fluorogens

[+] Author Affiliations
Tiziano Gaiotto, Hau B. Nguyen, Jaemyeong Jung, Gnana S. Gnanakaran, Jurgen G. Schmidt, Geoffrey S. Waldo, Andrew M. Bradbury, Peter M. Goodwin

Los Alamos National Lab. (USA)

Proc. SPIE 7905, Single Molecule Spectroscopy and Imaging IV, 79050O (February 10, 2011); doi:10.1117/12.875418
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From Conference Volume 7905

  • Single Molecule Spectroscopy and Imaging IV
  • Jörg Enderlein; Zygmunt K. Gryczynski; Rainer Erdmann
  • San Francisco, California, USA | January 22, 2011

abstract

We are exploring the use of fluorogen-activating proteins (FAPs) as reporters for single-molecule imaging. FAPs are single-chain antibodies selected to specifically bind small chromophoric molecules termed fluorogens. Upon binding to its cognate FAP the fluorescence quantum yield of the fluorogen increases giving rise to a fluorescent complex. Based on the seminal work of Szent-Gyorgyi et al. (Nature Biotechnology, Volume 26, Number 2, pp 235-240, 2008) we have chosen to study two fluorogen-activating single-chain antibodies, HL1.0.1-TO1 and H6-MG, bound to their cognate fluorogens, thiazole orange and malachite green derivatives, respectively. Here we use fluorescence correlation spectroscopy to study the photophysics of these fluorescent complexes.

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Citation

Tiziano Gaiotto ; Hau B. Nguyen ; Jaemyeong Jung ; Gnana S. Gnanakaran ; Jurgen G. Schmidt, et al.
"A photophysical study of two fluorogen-activating proteins bound to their cognate fluorogens", Proc. SPIE 7905, Single Molecule Spectroscopy and Imaging IV, 79050O (February 10, 2011); doi:10.1117/12.875418; http://dx.doi.org/10.1117/12.875418


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