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 Open

Presents the pdf analysis as premium feature

PDF Analysis

Insights

Presents the summarisation as premium feature

Summarisation

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

The electronic structure of charybdotoxin (ChTX), a scorpion venom peptidethat is known to act as a potassium channel blocker, is investigated with theaid of quantum mechanical calculations. The dipole moment vector (145 D) ofChTX can be stirred by the full length KcsA potassium channel's macrodipole(403 D) thereby assuming the proper orientation before binding the ion channelon the cell surface. The localization of the frontier orbitals of ChTX has beenrevealed for the first time. HOMO is localized on Trp14 while the threelowest-energy MOs (LUMO, LUMO+1, and LUMO+2) are localized on the threedisulfide bonds that characterize this pepetide. An effective way to engineerthe HOMO-LUMO (H-L) gap of ChTX is that of replacing its Trp14 residue withAla14 whereas deletion of the LUMO-associated disulfide bond with the insertionof a pair of L-alpha-aminobutyric acid residues does not affect the H-L energygap.

The electronic structure and dipole moment of charybdotoxin, a scorpion venom peptide with K+ channel blocking activity