Abstract
Hydrogen-deuterium exchange coupled to mass spectrometry is a powerful tool to evaluate changes in protein conformation between two or more states. Here, we describe a complete methodology that can be used to assess conformational changes in rhodopsin accompanying its transition from the inactive to activated state upon light exposure. This approach may be employed to investigate the structure and conformational changes of various membrane proteins.
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Acknowledgements
We would like to thank Dr. Malligarjunan Rajavel and Ms. Alicia Quick for their helpful comments and critical reading of the manuscript.
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Orban, T., Tsybovsky, Y. (2015). Probing Conformational Changes in Rhodopsin Using Hydrogen-Deuterium Exchange Coupled to Mass Spectrometry. In: Jastrzebska, B. (eds) Rhodopsin. Methods in Molecular Biology, vol 1271. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2330-4_8
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DOI: https://doi.org/10.1007/978-1-4939-2330-4_8
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Publisher Name: Humana Press, New York, NY
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