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Articles by Katherine Van
Allosteric Mechanisms of Non-Additive Substituent Contributions to Protein-Ligand Binding
Abstract Quantifying chemical substituent contributions to ligand binding free energies is challenging due to non-additive effects. Protein allostery is a frequent cause of non-additivity, but the underlying allosteric mechanisms often remain elusive. Here, we propose a general NMR-based approach to elucidate such mechanisms and we apply it to the HCN4 ion channel, whose cAMP-binding domain is an archetypal conformational switch.
Mechanism of allosteric inhibition in the Plasmodium falciparum cGMP-dependent protein kinase
Jung Ah Byun‡, Katherine Van‡, Jinfeng Huang§, Philipp Henning¶, Eugen Franz‖, Madoka Akimoto§, Friedrich W.
"Mechanism of Allosteric Inhibition in the Plasmodium falciparum cGMP-D" by Jung Ah Byun, Katherine Van et al.
Journal of Biological Chemistry 10.1074/jbc.RA120.013070 Post-print yes Allosteric Regulation, Binding Sites, Cyclic GMP, Cyclic GMP-Dependent Protein Kinases, Molecular Dynamics Simulation, Mutagenesis, Site-Directed, Nuclear Magnetic Resonance, Biomolecular, Plasmodium falciparum, Protein Domains, Protozoan Proteins, Recombinant Proteins, Surface Plasmon Resonance, cyclic GMP (cGMP), malaria, nuclear magnetic resonance (NMR), signaling, plasmodium, protein kinase G (PKG), 8-NBD-cGMP, CNB,...
An NMR based phosphodiesterase assay
An NMR based phosphodiesterase assay† You have access to this article Please wait while we load your content... Something went wrong. Try again?
Mechanism of allosteric inhibition in the
Jung Ah Byun1, Katherine Van2, Jinfeng Huang2, Philipp Henning3, Eugen Franz4, Madoka Akimoto5, Friedrich W.
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