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

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

2010-05-21

arxiv.org/abs/1005.3887v1

Computational and Theoretical Chemistry 963 (2011) 384-393

Biology

Quantitative Biology

Biomolecules

16 pages, 6 figures

Scientific paper

10.1016/j.comptc.2010.11.003

The electronic structure of charybdotoxin (ChTX), a scorpion venom peptide that is known to act as a potassium channel blocker, is investigated with the aid of quantum mechanical calculations. The dipole moment vector (145 D) of ChTX can be stirred by the full length KcsA potassium channel's macrodipole (403 D) thereby assuming the proper orientation before binding the ion channel on the cell surface. The localization of the frontier orbitals of ChTX has been revealed for the first time. HOMO is localized on Trp14 while the three lowest-energy MOs (LUMO, LUMO+1, and LUMO+2) are localized on the three disulfide bonds that characterize this pepetide. An effective way to engineer the HOMO-LUMO (H-L) gap of ChTX is that of replacing its Trp14 residue with Ala14 whereas deletion of the LUMO-associated disulfide bond with the insertion of a pair of L-alpha-aminobutyric acid residues does not affect the H-L energy gap.

Affiliated with

Also associated with

No associations

Rating

The electronic structure and dipole moment of charybdotoxin, a scorpion venom peptide with K+ channel blocking activity does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with The electronic structure and dipole moment of charybdotoxin, a scorpion venom peptide with K+ channel blocking activity, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and The electronic structure and dipole moment of charybdotoxin, a scorpion venom peptide with K+ channel blocking activity will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-339161