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A New Efficient Strategy to Reconstitute Membrane Proteins into Liposomes : Application to the Study of Ca++-Atpases

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Molecular Dynamics of Biomembranes

Part of the book series: NATO ASI Series ((ASIH,volume 96))

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Abstract

Reconstitution of integral membrane proteins into unilamellar phospholipid vesicles has played and should stay a potentially powerful tool to analyse structural as well as functional areas of membrane protein research. Although it is difficult to list all informations published since the pionering work of Racker and co-v/orkers initiated 20 years ago, a number of reviews are available including specific classes of membrane proteins such as receptors, substrate carriers, energy-conserving enzymes involved in oxidative phosphorylation and ion motive ATPases (Racker, 1979; Eytan, 1982; Casey, 1984; Levitzki, 1985; Jain and Zakim, 1987; Villalobo, 1990; Cornelius, 1991; Rigaud et al, 1995).

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© 1996 Springer-Verlag Berlin Heidelberg

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Rigaud, JL., Levy, D. (1996). A New Efficient Strategy to Reconstitute Membrane Proteins into Liposomes : Application to the Study of Ca++-Atpases. In: Op den Kamp, J.A.F. (eds) Molecular Dynamics of Biomembranes. NATO ASI Series, vol 96. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61126-1_30

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  • DOI: https://doi.org/10.1007/978-3-642-61126-1_30

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