Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 65458
Title Fluorescence dynamics of green fluorescent protein in AOT reversed micelles
Author(s) Uskova, M.A.; Borst, J.W.; Hink, M.A.; Hoek, A. van; Schots, A.; Klyachko, N.L.; Visser, A.J.W.G.
Source Biophysical Chemistry 87 (2000). - ISSN 0301-4622 - p. 73 - 84.
DOI http://dx.doi.org/10.1016/S0301-4622(00)00184-8
Department(s) Biochemistry
Biophysics
Laboratory of Nematology
EPS
Publication type Refereed Article in a scientific journal
Publication year 2000
Abstract We have used the enhanced green fluorescent protein (EGFP) to investigate the properties of surfactant-entrapped water pools in organic solvents (reversed micelles) with steady-state and time-resolved fluorescence methods. The surfactant used was sodium bis(2-ethylhexyl)sulfosuccinate (AOT) and the organic solvents were isooctane and (the more viscous) dodecane, respectively. The water content of the water pools could be controlled through the parameter w0, which is the water-to-surfactant molar ratio. With steady-state fluorescence, it was observed that subtle fluorescence changes could be noted in reversed micelles of different water contents. EGFP can be used as a pH-indicator of the water droplets in reversed micelles. Time- resolved fluorescence methods also revealed subtle changes in fluorescence decay times when the results in bulk water were compared with those in reversed micelles. The average fluorescence lifetimes of EGFP scaled with the relative fluorescence intensities. Time-resolved fluorescence anisotropy of EGFP in aqueous solution and reversed micelles yielded single rotational correlation times. Geometrical considerations could assign the observed correlation times to dehydrated protein at low w0 and internal EGFP rotation within the droplet at the highest w0. (C)
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