This paper describes three protocols for identifying interacting surfaces on 15N-labeled target proteins of known structure by using in-cell NMR spectroscopy. The first protocol describes how to identify protein quinary structure interaction surfaces in prokaryotes by using cross-relaxation-induced polarization transfer, CRIPT, based in-cell NMR. The second protocol describes how to introduce labeled protein into eukaryotic (HeLa) cells via electroporation for CRIPT-based in-cell studies. The third protocol describes how to quantitatively map protein interacting surfaces by utilizing singular value decomposition, SVD, analysis of STructural INTeractions by in-cell NMR, STINT-NMR, data.
CITATION STYLE
Burz, D. S., DeMott, C. M., Aldousary, A., Dansereau, S., & Shekhtman, A. (2018). Quantitative determination of interacting protein surfaces in prokaryotes and eukaryotes by using in-cell NMR spectroscopy. In Methods in Molecular Biology (Vol. 1688, pp. 423–444). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7386-6_20
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