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.
CITATION STYLE
Thompson, P. M., Beck, M. R., & Campbell, S. L. (2015). Protein-protein interaction analysis by nuclear magnetic resonance spectroscopy. In Protein-Protein Interactions: Methods and Applications: Second Edition (pp. 267–279). Springer New York. https://doi.org/10.1007/978-1-4939-2425-7_16
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