Abstract
NMR spectroscopy and other solution methods are increasingly being used to obtain novel insights into the mechanisms by which MAPK regulatory proteins bind and direct the activity of MAPKs. Here, we describe how interactions between the MAPK p38α and its regulatory proteins are studied using NMR spectroscopy, isothermal titration calorimetry, and small angle X-ray scattering (SAXS).
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Acknowledgement
The authors thank the large numbers of highly skilled and ambitious coworkers for their strong support in the effort to better understand protein phosphatases. They are also deeply indebted to many members of the phosphatase field—too many to name—for their support, for their collaborations and their input. We thank Dr. Michael Clarkson (Brown University) for input for the document and Dr. Andrew Hink (UTHSCSA) for input in regard to D2O recycling. This work was supported by NIH grant R01GM098482 to RP, R01GM100910 to WP.
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Peti, W., Page, R. (2016). NMR Spectroscopy to Study MAP Kinase Binding to MAP Kinase Phosphatases. In: Pulido, R. (eds) Protein Tyrosine Phosphatases. Methods in Molecular Biology, vol 1447. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-3746-2_11
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DOI: https://doi.org/10.1007/978-1-4939-3746-2_11
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