A photophysical study of two fluorogen-activating proteins bound to their cognate fluorogens [electronic resource]

• Ngôn ngữ: eng
• Ký hiệu phân loại: 541.3 Miscellaneous topics in physical chemistry
• Thông tin xuất bản: Los Alamos, N.M. : Oak Ridge, Tenn. : Los Alamos National Laboratory ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2010
• Mô tả vật lý: Medium: ED : , digital, PDF file.
• Bộ sưu tập: Metadata
• ID: 262376
• Chủ đề: 1. 37 inorganic, organic, physical and analytical chemistry; 2. 59 basic biological sciences; 3. 60 applied life sciences; 4. Antibodies; 5. Biotechnology; 6. Fluorescence; 7. Oranges; 8. Proteins; 9. Spectroscopy; 10. Thiazoles

Tóm tắt

We are exploring the feasibility of using recently developed flu orogen-activating proteins (FAPs) as reporters for single-molecule imaging. FAPs are single-chain antibodies choosen to specifically bind small chromophoric molecules termed f1uorogens. Upon binding to its cognate FAP the fluorescence quantum yield of the fluorogen can increase substantially 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, HL 1.0.1-TOI and H6-MG bound to their cognate fluorogens, thiazole orange and malachite green derivatives, respectively. Here we use fluorescence correlation spectroscopy study the photophysics of these fluorescent complexes.