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Bacterial Protein Secretion Systems pp 277–287Cite as

Assessing Energy-Dependent Protein Conformational Changes in the TonB System

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 1615))

Abstract

Changes in conformation can alter a protein’s vulnerability to proteolysis. Thus, in vivo differential proteinase sensitivity provides a means for identifying conformational changes that mark discrete states in the activity cycle of a protein. The ability to detect a specific conformational state allows for experiments to address specific protein–protein interactions and other physiological components that potentially contribute to the function of the protein. This chapter presents the application of this technique to the TonB-dependent energy transduction system of Gram-negative bacteria, a strategy that has refined our understanding of how the TonB protein is coupled to the ion electrochemical gradient of the cytoplasmic membrane.

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Author information

Authors and Affiliations

  1. Department of Biological Sciences, Bowling Green State University, Bowling Green, OH, 43403, USA

    Ray A. Larsen

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  1. Ray A. Larsen
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Correspondence to Ray A. Larsen .

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Editors and Affiliations

  1. Institut de Microbiologie de la Méditerranée, Aix-Marseille Univ - CNRS, Marseille, France

    Laure Journet

  2. Institut de Microbiologie de la Méditerranée, Aix-Marseille Univ - CNRS, Marseille, France

    Eric Cascales

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Larsen, R.A. (2017). Assessing Energy-Dependent Protein Conformational Changes in the TonB System. In: Journet, L., Cascales, E. (eds) Bacterial Protein Secretion Systems. Methods in Molecular Biology, vol 1615. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7033-9_22

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  • DOI: https://doi.org/10.1007/978-1-4939-7033-9_22

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-7031-5

  • Online ISBN: 978-1-4939-7033-9

  • eBook Packages: Springer Protocols

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