11 February 2011 A photophysical study of two fluorogen-activating proteins bound to their cognate fluorogens
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Proceedings Volume 7905, Single Molecule Spectroscopy and Imaging IV; 79050O (2011); doi: 10.1117/12.875418
Event: SPIE BiOS, 2011, San Francisco, California, United States
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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Tiziano Gaiotto, Hau B. Nguyen, Jaemyeong Jung, Gnana S. Gnanakaran, Jurgen G. Schmidt, Geoffrey S. Waldo, Andrew M. Bradbury, Peter M. Goodwin, "A photophysical study of two fluorogen-activating proteins bound to their cognate fluorogens", Proc. SPIE 7905, Single Molecule Spectroscopy and Imaging IV, 79050O (11 February 2011); doi: 10.1117/12.875418; https://doi.org/10.1117/12.875418
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KEYWORDS
Proteins

Fluorescence correlation spectroscopy

Luminescence

Diffusion

Imaging spectroscopy

Molecules

Avalanche photodetectors

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