Important biological processes, including enzyme catalysis, signaling, and protein folding, proceed through lowly populated (<5%) states that elude structural characterization by conventional techniques. Here, we describe the steps required for visualization of these sparsely populated conformations and transient protein-protein interactions using paramagnetic relaxation enhancement solution NMR. We describe experimental design, sample preparation, data acquisition and processing, and the basics of data analysis of structural ensembles.
CITATION STYLE
Venditti, V., & Fawzi, N. L. (2018). Probing the atomic structure of transient protein contacts by paramagnetic relaxation enhancement solution NMR. In Methods in Molecular Biology (Vol. 1688, pp. 243–255). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7386-6_12
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