Solution structure of the potassium channel scorpion toxin HSTX1
Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: solution structure of the potassium channel inhibitor HsTX1.
A four-disulfide-bridged toxin, with high affinity towards voltage-gatedc K+ channels, isolated from Heterometrus spinnifer (scorpionidae) venom
Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels.
Purification, characterization, and synthesis of three novel toxins from the Chinese scorpion Buthus martensi, which act on K+ channels
SOLID PHASE CHEMICAL SYNTHESIS USING THE FMOC METHODOLOGY. THE SEQUENCE OF THIS PEPTIDE OCCURS NATURALLY IN SCORPIONS (SCORPIONIDAE).
A COMPLETLY EXTENDED CONFORMATION WAS USED AS THE STARTING STRUCTURE. 25 ITERATIONS WERE MADE. 500 STRUCTURES WERE CALCULATED. RESTRAINED MOLECULAR DYNAMICS AT 600K A SLOW COOLING. MINIMIZATION WERE MADE WITH AN ELECTROSTATIC TERM TOPALLH22X.PRO AND PARALLH22X.PRO
SCORPION TOXIN, ALPHA BETA, MOLECULAR MODELING, POTASSIUM CHANNEL, TOXIN