Thread: NMR paper Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure
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Default Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure
Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure

Proteins undergo changes in their partial volumes in numerous biological processes such as enzymatic catalysis, unfolding-refolding, and ligand binding. The change in the protein volume upon ligand binding-a parameter termed the protein-ligand binding volume-can be extensively studied by high-pressure NMR spectroscopy. In this study, we developed a method to determine the protein-ligand binding volume from a single two-dimensional (2D) ¹H-^(15)N heteronuclear single quantum coherence (HSQC)...

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