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Fluorescence study of cytochrome C complexes with phospholipids

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Spectroscopy of Biological Molecules: New Directions
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Abstract

Model systems containing peripheral protein of mitochondrial membrane cytochrome C (cyt c) and liposomes of various composition are presently extensively used in elucidating the mechanisms of protein-lipid interactions [1]. One approach to obtain structural information on such systems is based on the monitoring fluorescence energy transfer (FET) [2, 3]. In the previous FET study of cyt c interaction with liposomes an assumption has been made concerning the existence of preferential protein orientation with respect to the surface of negatively charged model membranes [4]. In the present work FET technique has been employed to gain additional arguments in favour of this assumption.

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References

  1. Sankaram M.B. and Marsh D., In Watts A (Ed.) Protein — Lipid Interactions, Elsevier, 1993, pp. 127–162.

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© 1999 Springer Science+Business Media Dordrecht

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Gorbenko, G.P. (1999). Fluorescence study of cytochrome C complexes with phospholipids. In: Greve, J., Puppels, G.J., Otto, C. (eds) Spectroscopy of Biological Molecules: New Directions. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4479-7_163

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  • DOI: https://doi.org/10.1007/978-94-011-4479-7_163

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-5919-0

  • Online ISBN: 978-94-011-4479-7

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