English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

Xenon can produce general anesthesia. Its main protein target is theN-methyl-D-aspartate receptor, a ionotropic channel playing a pivotal role inthe function of the central nervous system.  The molecular mechanisms allowing this noble gas to have such a specificeffect remain obscure, probably as a consequence of the lack of structural dataat the atomic level of detail. Herein, as a result of five independentmolecular dynamics simulations, three different binding sites were found forxenon in the glycine binding domain of the N-methyl-D-aspartate receptor. Theabsolute binding free energy of xenon in these sites ranges between -8 and -14kJ/mole. However, it depends significantly upon the protein conformer chosenfor performing the calculation, suggesting that larger values could probably beobtained, if other conformers were considered.  These three sites are next to each other, one of them being next to theglycine site. This could explain why the F758W and F758Y mutations can preventcompetitive inhibition by xenon without affecting glycine binding.

At least three xenon binding sites in the glycine binding domain of the N-methyl D-aspartate receptor