Fluorescence quenching in protein-lipid system: contribution of diffusion-controlled factors
Keywords:
quenching ofprotein fluorescence, diffusion of lipid-bound protein, quenching rate constant
Abstract
Using the model of diffusion-controlled reactions between asymmetric species the quenching of the protein fluorescence by extrinsic quenchers has been considered. The changes in bimolecular quenching rate constant stemming from the protein immobilization on the surface of lipid vesicles have been evaluated. It has been shown that association of the proteins whose radius is less than 2 nm with lipid vesicles can be followed by the apparent decrease of the quenching efficiency due to reduced translational and rotational diffusion coefficients of the bound protein.
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References
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Sankaram M, Marsh D. Protein-Lipid Interactions. Elsevier; 1993. p. 127-62.
Lakowicz JR. Principles of fluorescent spectroscopy. New York: Plenum Press; 1999.
Johnson DA, Yguerabide J. Biophys J. 1985;949-55.
Shoup D, Lipari G, Szabo A. Ibid. 1981;697-714.
Kostiuk PG, Grodzinskii DM, Zima VL. Kiev:Vyshcha shkola; 1988, 503p.
Erdey-Gruz T. Transport phenomena in aqueous solutions. New York:John Wiley and Sons, Inc; 1974.
Gamolina OV, Gorbenko GP, Domanov YeA. Biophysical Bulletin. 2002;10(1):124-6.
Published
2018-06-25
Cited
How to Cite
Domanov, Y. A., Gorbenko, G. P., & Gamolina, O. V. (2018). Fluorescence quenching in protein-lipid system: contribution of diffusion-controlled factors. Biophysical Bulletin, 1(12), 117-119. Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/12153
Section
Methods of biophysical investigations
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