NMR reveals novel mechanisms of protein activity regulation
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TLDR
A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.Abstract:
NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide site-resolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.read more
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Dynamic allostery: linkers are not merely flexible.
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Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle
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The design of covalent allosteric drugs.
Ruth Nussinov,Chung-Jung Tsai +1 more
TL;DR: In a recent promising step in therapeutic drug development, allosteric, disulfide-tethered fragments successfully modulated the activity of a protein kinase and K-Ras.
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Advances in NMR Methods To Map Allosteric Sites: From Models to Translation
TL;DR: It is clear that NMR plays a central role not only in experimentally validating transformative theories of allostery, but also in tapping the full translational potential of allosteric systems.
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