Ligand-specific changes in conformational flexibility mediate long-range allostery in the lac repressor
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DOI: 10.1038/s41467-023-36798-1
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References listed on IDEAS
- Xian-Li Jiang & Rey P. Dimas & Clement T. Y. Chan & Faruck Morcos, 2021. "Coevolutionary methods enable robust design of modular repressors by reestablishing intra-protein interactions," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
- Ryan E Pavlovicz & Hahnbeom Park & Frank DiMaio, 2020. "Efficient consideration of coordinated water molecules improves computational protein-protein and protein-ligand docking discrimination," PLOS Computational Biology, Public Library of Science, vol. 16(9), pages 1-20, September.
- Javier F. Juárez & Begoña Lecube-Azpeitia & Stuart L. Brown & Christopher D. Johnston & George M. Church, 2018. "Biosensor libraries harness large classes of binding domains for construction of allosteric transcriptional regulators," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
- Daniel J Parente & Liskin Swint-Kruse, 2013. "Multiple Co-Evolutionary Networks Are Supported by the Common Tertiary Scaffold of the LacI/GalR Proteins," PLOS ONE, Public Library of Science, vol. 8(12), pages 1-17, December.
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