Abstract
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.
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Acknowledgments
Research reported in this publication was supported in part by the National Institute Of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) under Award Number R01GM118530 (to N.L.F) and by startup funding from Iowa State University (to V.V.).
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Venditti, V., Fawzi, N.L. (2018). Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR. In: Ghose, R. (eds) Protein NMR. Methods in Molecular Biology, vol 1688. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7386-6_12
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DOI: https://doi.org/10.1007/978-1-4939-7386-6_12
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