The interactions between a molecule and the aqueous environment underpin any process
that occurs in solution, from simple chemical reactions to protein–ligand binding to protein …

The four N-methyl-d-aspartate (NMDA) receptor NR2 subunits (NR2A-D) have different
developmental, anatomical, and functional profiles that allow them to serve different roles in …

We have used site-directed mutagenesis of amino acids located within the S1 and S2 ligand
binding domains of the NR2A N-methyl-d-aspartate (NMDA) receptor subunit to explore the …

The computational prediction of protein–ligand binding affinities is of central interest in early-stage
drug-discovery, and there is a widely recognized need for improved methods. Low …

Heteromeric NMDARs are composed of coagonist glycine‐binding NR1 subunits and
glutamate‐binding NR2 subunits. The majority of functional NMDARs in the mammalian central …

We have studied relative efficacies of NR1 agonists glycine and d-cycloserine (DCS), and
found efficacy to be dependent on the NR2 subunit. DCS shows partial agonism at NR1/NR2B …

Prediction of the free energy of solvation of a small molecule, or its transfer energy, is a
necessary step along the path towards calculating the interactions between molecules that occur …

The NMDA ionotropic glutamate receptor is ubiquitous in mammalian central neurons.
Because partial agonists bind to the same site as glutamate but induce less channel activation, …

Zinc is hypothesized to be co-released with glutamate at synapses of the central nervous
system. Zinc binds to NR1/NR2A N-methyl-d-aspartate (NMDA) receptors with high affinity and …

Knowledge of and information about protein binding sites has become increasingly important
in the drug discovery process and not just for molecular biologists [1]. By comparing …