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Spectroscopic Studies of Rotational Diffusion and Protein-Protein Interactions in Biological Membranes

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Reactions in Compartmentalized Liquids
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Abstract

Rotational diffusion of proteins in membranes may be measured by observing flash-induced transient dichroism of triplet probes or intrinsic chromophores. Measurements with bacteriorhodopsin reconstituted into dimyristoylphosphatidyleholine vesicles are in good agreement with a model in which rotation of the protein only occurs about the membrane normal. Combination of rotational and lateral diffusion measurements enables calculation of a value for the protein diameter which is in good agreement with that obtained by electron microscopy.

The rotational diffusion of the anion transport protein, band 3, has been measured in the human erythrocyte membrane. This system has been used to investigate the action of melittin, a potent lytic polypeptide from bee venom. It was found that melittin strongly reduces the rotational mobility of band 3 by promoting protein aggregation. It is suggested that such protein aggregation may play a role in melittin’s lytic activity.

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© 1989 Springer-Verlag Berlin Heidelberg

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Cherry, R.J. (1989). Spectroscopic Studies of Rotational Diffusion and Protein-Protein Interactions in Biological Membranes. In: Knoche, W., Schomäcker, R. (eds) Reactions in Compartmentalized Liquids. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74787-8_11

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  • DOI: https://doi.org/10.1007/978-3-642-74787-8_11

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-51188-5

  • Online ISBN: 978-3-642-74787-8

  • eBook Packages: Springer Book Archive

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