Abstract
Fragment-based screening by ligand-observed 1D NMR and binding interface map** by protein-observed 2D NMR are popular methods used in drug discovery. These methods allow researchers to detect compound binding over a wide range of affinities and offer a simultaneous assessment of solubility, purity, and chemical formula accuracy of the target compounds and the 15N-labeled protein when examined by 1D and 2D NMR, respectively. These methods can be applied for screening fragment binding to the active (GMPPNP-bound) and inactive (GDP-bound) states of oncogenic KRAS mutants.
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Acknowledgments
This project was funded in part with federal funds from the National Cancer Institute, National Institutes of Health under contract 75N91019D00024. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, and the mention of trade names, commercial products, or organizations does not imply endorsement by the US government.
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Cornilescu, G. (2024). 1D and 2D NMR for KRAS:Ligand Binding. In: Stephen, A.G., Esposito, D. (eds) KRAS. Methods in Molecular Biology, vol 2797. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3822-4_9
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DOI: https://doi.org/10.1007/978-1-0716-3822-4_9
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