Quantifying Water-Mediated Protein-Ligand Interactions in a Glutamate Receptor

Quantifying Water-Mediated Protein–Ligand Interactions in a Glutamate Receptor: A DFT Study

It is becoming increasingly clear that careful treatment of water molecules in ligand-protein interactions is required in many cases if the correct binding pose is to be identified in molecular docking. Water can form complex bridging networks and can play a critical role in dictating the binding mode of ligands. A particularly striking example of this can be found in the ionotropic glutamate r...

Ligand Recognition in SH3-mediated Protein Interactions

Hyperpolarized Water to Study Protein-Ligand Interactions.

The affinity between a chosen target protein and small molecules is a key aspect of drug discovery. Screening by popular NMR methods such as Water-LOGSY suffers from low sensitivity and from false positives caused by aggregated or denatured proteins. This work demonstrates that the sensitivity of Water-LOGSY can be greatly boosted by injecting hyperpolarized water into solutions of proteins and...

Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry.

A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein-ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand binding. A reference ligand (L(ref)), which binds specifically to the protein (P), at the same bind...

Protein-blot analysis of receptor-ligand interactions.

Protein blotting was originally introduced as a solid-phase immunoassay (Gershoni & Palade, 1983; Towbin & Gordon, 1984). However, this technique can also be employed for the analysis of ligand-receptor interactions. In principle, a protein sample containing a receptor is resolved by gel electrophoresis and then blotted to an immobilizing matrix, such as a nitrocellulose membrane filter, as wou...