Abstract
Nuclear magnetic resonance (NMR) has continued to evolve as a powerful method, with an increase in the number of pulse sequences and techniques available to study protein-protein interactions. In this chapter, a straightforward method to map a protein–protein interface and design a structural model is described, using chemical shift perturbation, paramagnetic relaxation enhancement, and data-driven docking.
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Thompson, P.M., Beck, M.R., Campbell, S.L. (2015). Protein-Protein Interaction Analysis by Nuclear Magnetic Resonance Spectroscopy. In: Meyerkord, C., Fu, H. (eds) Protein-Protein Interactions. Methods in Molecular Biology, vol 1278. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2425-7_16
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DOI: https://doi.org/10.1007/978-1-4939-2425-7_16
Publisher Name: Humana Press, New York, NY
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