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Isothermal Titration Calorimetry of Membrane Proteins

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Structure and Function of Membrane Proteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2302))

Abstract

The ability to quantify protein–protein interactions without adding labels to protein has made isothermal titration calorimetry (ITC) a preferred technique to study proteins in aqueous solution. Here, we describe the application of ITC to the study of protein–protein interactions in membrane mimics using the association of integrin αIIb and β3 transmembrane domains in phospholipid bicelles as an example. A higher conceptual and experimental effort compared to water-soluble proteins is required for membrane proteins and rewarded with rare thermodynamic insight into this central class of proteins.

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Acknowledgments

This work was supported by NIH grant R03AG063284 and American Heart Association Grant #18TPA34170481 to T.S.U.

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Correspondence to Tobias S. Ulmer .

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Vu, H.N., Situ, A.J., Ulmer, T.S. (2021). Isothermal Titration Calorimetry of Membrane Proteins. In: Schmidt-Krey, I., Gumbart, J.C. (eds) Structure and Function of Membrane Proteins. Methods in Molecular Biology, vol 2302. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1394-8_5

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  • DOI: https://doi.org/10.1007/978-1-0716-1394-8_5

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-1393-1

  • Online ISBN: 978-1-0716-1394-8

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