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Introduction

  • Chapter
Proteins Membrane Binding and Pore Formation

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 677))

Abstract

Pore-forming proteins (PFPs) possess the intriguing property that they can exist either in a stable water-soluble state or as an integral membrane pore. These molecules can undergo large conformational changes in converting between these two states. Much of what we know about how these proteins change their shape comes from work on bacterial toxins and increasingly, in more recent years, on toxins from other organisms. Surprisingly, a number of pore-forming proteins have recently been characterised that appear to have adopted similar stratagies to toxins for binding and inserting into biological membranes.

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Authors and Affiliations

  1. St. Vincent’s Institute of Medical Research, 9 Princes Street, Fitzroy, Victoria, 3065, Australia

    Susanne C. Feil, Galina Polekhina, Michael A. Gorman & Michael W. Parker

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  1. Susanne C. Feil
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  2. Galina Polekhina
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  3. Michael A. Gorman
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  4. Michael W. Parker
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Correspondence to Michael W. Parker .

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Editors and Affiliations

  1. Department of Biology, University of Ljubljana, Ljubljana, Slovenia

    Gregor Anderluh PhD

  2. Institute for Cell and Molecular Biosciences, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne, UK

    Jeremy Lakey PhD

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Feil, S.C., Polekhina, G., Gorman, M.A., Parker, M.W. (2010). Introduction. In: Anderluh, G., Lakey, J. (eds) Proteins Membrane Binding and Pore Formation. Advances in Experimental Medicine and Biology, vol 677. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6327-7_1

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