Chapter title |
Assessing Energy-Dependent Protein Conformational Changes in the TonB System
|
---|---|
Chapter number | 22 |
Book title |
Bacterial Protein Secretion Systems
|
Published in |
Methods in molecular biology, July 2017
|
DOI | 10.1007/978-1-4939-7033-9_22 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7031-5, 978-1-4939-7033-9
|
Authors |
Ray A. Larsen, Larsen, Ray A. |
Editors |
Laure Journet, Eric Cascales |
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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